histidine has been researched along with nad in 162 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 76 (46.91) | 18.7374 |
1990's | 39 (24.07) | 18.2507 |
2000's | 35 (21.60) | 29.6817 |
2010's | 8 (4.94) | 24.3611 |
2020's | 4 (2.47) | 2.80 |
Authors | Studies |
---|---|
Hiwatashi, A; Ichikawa, Y; Maruya, N; Yamano, T | 1 |
Dickenson, CJ; Dickinson, FM | 3 |
Hack, E; Kemp, JD | 1 |
Fan, CC; Plaut, GW; Stegeman, WJ | 1 |
Holbrook, JJ; Jeck, R; Lodola, A; Parker, DM | 1 |
Holbrook, JJ; Lodola, A; Parker, DM | 1 |
Leskovac, V; Pavkov-Pericin, D | 1 |
Allen, G; Harris, JI | 1 |
Berezin, IV; Egorov, AM; Popov, VO | 1 |
Gregory, EM | 1 |
Kim, H; Patel, MS | 1 |
Colman, RF; Ehrlich, RS | 1 |
Galloway, DR; Kessler, SP | 1 |
Cook, JM; Iglewski, BH; Wick, MJ | 1 |
Kamiński, ZW; Zakrzewska, B | 1 |
Bhaduri, A; Mukherji, S | 1 |
Anderson, DC; Galloway, DR; Kessler, SP; McGowan, JL | 1 |
Bosron, WF; Edenberg, HJ; Ehrig, T; Hurley, TD | 1 |
Kanofsky, JR; Sima, P | 1 |
Gould, RM; Plapp, BV | 1 |
Montecucco, C; Papini, E; Rappuoli, R; Schiavo, G | 1 |
Hove-Jensen, B | 1 |
Montecucco, C; Papini, E; Rappuoli, R; Sandoná, D; Schiavo, G | 1 |
Kim, HS; Legoy, MD; Minard, P; Thomas, D | 1 |
Carrea, G; Mazzola, G; Pasta, P | 1 |
Baijal, M; Sane, PV | 1 |
Beppu, T; Iijima, S; Oh, MJ; Saiki, T | 1 |
Cook, PF; Harris, BG; Rao, JG | 1 |
Schäfer, R; Schwartz, AC | 1 |
Carter, JG; Lowry, OH | 1 |
Berghäuser, J; Jeck, R; Woenckhaus, C; Zoltobrocki, M | 1 |
Coote, JG; Hassall, H | 1 |
Zajac, J | 1 |
Brosemer, RW; Kuhn, RW | 1 |
Kobayashi, S; Sekine, T; Yamashita, T | 1 |
Bray, DF; Kapoor, M; Ward, GW | 1 |
Apitz-Castro, R; Suarez, Z | 1 |
Bond, JS; Francis, SH; Park, JH | 1 |
Keleti, T; Ovádi, J | 1 |
Kaback, HR; Milner, LS | 1 |
Batke, J; Keleti, T | 1 |
Anderton, BH; Rabin, BR | 1 |
Berghäuser, J; Falderbaum, I; Woenckhaus, C | 1 |
Bruni, CB; Rechler, MM | 1 |
Yamaguchi, T | 1 |
Dénes, G; Patthy, L | 1 |
Thomas, P; Tudball, N | 1 |
Gregory, EM; Harrison, JH; Rohrbach, MS | 1 |
Brooks, RL; Shore, JD | 1 |
Arias, F; Sweet, F; Warren, JC | 1 |
Branefors-Helander, P | 1 |
Fenselau, A; Moore, J | 1 |
McKinley-McKee, JS; Morris, DL | 1 |
Bailey-Wood, R; Thomas, P; Tudball, N | 1 |
Francis, SH; Meriwether, BP; Park, JH | 2 |
Hucho, F; Markau, U; Sund, H | 1 |
MacLeod, RA; Rogers, HJ; Thurman, P | 1 |
Scott, MD; Sykes, BD | 1 |
Danson, MJ; Weitzman, PD | 2 |
Holbrook, JJ; Wallis, RB | 1 |
Holbrook, JJ; Ingram, VA | 1 |
Holbrook, JJ; Stinson, RA | 1 |
Ballio, A; Carere, A; Russi, S; Siracusano, A | 1 |
Carper, WR; Maijub, AG; Miller, GR; Pecht, MA | 1 |
Das, S; Marshall, FD; Skaper, SD | 1 |
Emes, AV; Hassall, H | 1 |
Barbieri, G; Gagliano, R; Grazi, E | 1 |
Foster, M; Harrison, JH | 1 |
Holbrook, JJ; Illsley, NP; Lodola, A | 1 |
Gaudemer, Y; Latruffe, N | 1 |
Carper, WR; Thompson, RE | 1 |
Harrison, JH; Hodges, CT; Jurgensen, SR | 1 |
Hennecke, M; Plapp, BV | 1 |
Bodley, JW; Dunlop, PC; VanNess, BG | 1 |
Hatefi, Y; Vik, SB | 1 |
Fujioka, M; Gomi, T | 1 |
Heard, JT; Steiner, BM; Tritz, GJ | 1 |
Bürger, E; Görisch, H | 1 |
Cui, K; Lu, AY; Ma, Q; Yang, CS | 1 |
Barriault, D; Hurtubise, Y; Powlowski, J; Sylvestre, M | 1 |
Furumo, NC; Helton, M; Milbrandt, J; Rardin, J; Wright, SK; Zhao, FJ | 1 |
Hu, X; Persson, A; Rydström, J; Zhang, JW | 1 |
Miyazaki, K; Oshima, T; Yaoi, T | 1 |
Domenighini, M; Magagnoli, C; Pizza, M; Rappuoli, R | 1 |
Dekker, EE; Marcus, JP | 1 |
Li, Y; Man, WJ; O'Connor, CD; Wilton, DC | 1 |
Iwasaki, G; Kheirolomoom, A; Mano, J; Nagai, A; Ogawa, A; Ohta, D | 1 |
Barbançon-Finck, V; Barbieri, JT; Xu, Y | 1 |
Blanke, SR; Collier, RJ; Covacci, A; Huang, K; Papini, E; Wilson, BA | 1 |
Eklund, H; Plapp, BV; Ramaswamy, S | 1 |
Nagai, A; Ohta, D | 1 |
Bülow, L; Carlsson, H; Prachayasittikul, V | 1 |
Dannelly, HK; Roseman, S | 1 |
Aiba, H; Mizuno, T; Ohmiya, R; Yamada, H | 1 |
Farrar, JA; Formicka, G; Thomson, AJ; Zeppezauer, M | 1 |
Eulitz, M; Hlavica, P; Lehnerer, M | 1 |
Bragg, PD; Hou, C | 2 |
Altenbuchner, J; Brünker, P; Kulbe, KD; Mattes, R | 1 |
Buchlow, G; Griesenbeck, J; Mayer-Kuckuk, P; Oei, SL; Schweiger, M; Ziegler, M | 1 |
Nadolny, C; Zundel, G | 1 |
Beber, FA; Brigo, MJ; Pereira, CN; Rocha, JB; Silva, MC; Wollmeister, J | 1 |
Adler, S; Blanco, G; Evans, BW; Isenberg, KE; Mason, JI; Mercer, RW; Nash, WE; Strickler, RC; Thomas, JL | 1 |
Brady, RL; Chapman, AD; Clarke, AR; Cortés, A; Dafforn, TR | 1 |
Bertoloni, G; Jori, G; Polo, L; Presti, F; Schindl, A; Schindl, L | 1 |
LeBrun, LA; Plapp, BV | 1 |
Moynihan, DP; Parikh, S; Tonge, PJ; Xiao, G | 1 |
Delley, M; Germond, JE; Hottinger, H; Kochhar, S; Lamzin, VS; Razeto, A | 1 |
Doehr, O; Gutierrez, A; Paine, M; Roberts, GC; Scrutton, NS; Wolf, CR | 1 |
Azzi, A; Bellemare, V; Chang, HJ; Huang, YW; Laberge, S; Lin, SX; Pineau, I | 1 |
Shuman, S; Sriskanda, V | 1 |
Barbosa, JA; Cygler, M; Larocque, R; Li, Y; Matte, A; Schrag, JD; Sivaraman, J | 1 |
Balducci, E; Micossi, LG | 1 |
Jonson, PH; Londesborough, J; Penttilä, M; Richard, P; Sundqvist, L; Verho, R | 1 |
Pai, EF; Saridakis, V | 1 |
Bonete, MJ; Díaz, S; Ferrer, J; Oren, A; Pérez-Pomares, F | 1 |
ALIVISATOS, SG; CALLAGHAN, O; UNGAR, F | 1 |
SHIFRIN, S | 1 |
DOBRY-DUCLAUX, A | 1 |
MAGASANIK, B; SCHLESINGER, S | 1 |
BOYER, PD; DUFFY, JJ; LINDBERG, O; NORMAN, AW | 1 |
Anderson, RM; Howitz, KT; Latorre-Esteves, M; Lavu, S; Medvedik, O; Neves, AR; Santos, H; Sinclair, DA; Taylor, C | 1 |
Popov, VO; Savel'eva, ND; Tikhonova, TV | 1 |
Londesborough, J; Penttilä, M; Putkonen, M; Richard, P; Verho, R | 1 |
LeBrun, LA; Park, DH; Plapp, BV; Ramaswamy, S | 1 |
Fujiwara, S; Kawamura, K; Takabayashi, T; Takahashi, F; Yubisui, T | 1 |
Bordelon, T; Montegudo, SK; Newcomer, ME; Oldham, ML; Pakhomova, S | 1 |
Chen, E; Goldbeck, RA; Kliger, DS | 1 |
Russell, TR; Tu, SC | 1 |
Abdrakhmanova, A; Brandt, U; Kerscher, S; Waletko, A; Zickermann, V; Zwicker, K | 1 |
Contreras-Shannon, V; Lin, AP; McAlister-Henn, L; McCammon, MT | 1 |
Kodaki, T; Makino, K; Watanabe, S | 1 |
Boswell, EL; Pletnev, V; Scaccia, LA; Thomas, JL; Umland, TC | 1 |
Callender, R; McClendon, S; Zhadin, N | 1 |
Adisa, A; Alpyurek, AE; Colman, PM; Klonis, N; Luo, CS; Malby, RL; Satchell, JF; Smith, BJ; Tilley, L | 1 |
Chin, F; Gassner, GT; Kantz, A; Nallamothu, N; Nguyen, T | 1 |
Barros, MH; Clarke, CF; Gin, P; Johnson, A; Marbois, BN; Tzagoloff, A | 1 |
Denu, JM; Smith, BC | 1 |
Wang, S; Yu, H | 1 |
Aliverti, A; Coda, A; de Rosa, M; Mattevi, A; Pandini, V; Pennati, A; Razeto, A; Vanoni, MA; Zanetti, G | 1 |
Karagüler, NG; Ordu, EB | 1 |
Fukuzumi, S; Yamada, S; Yuasa, J | 1 |
Kinoshita, K; Oshima, T; Shida, Y; Shimizu, M; Yamagishi, A | 1 |
Al-Shawi, MK; Nakamoto, RK; Scanlon, JA | 1 |
Ioerger, TR; Kuppan, G; Owen, JL; Reddy, MC; Sacchettini, JC; Shetty, ND | 1 |
Bonvin, J; Christendat, D; Hou, W; Kimber, MS; Shahinas, D; Sun, W; Turnbull, J | 1 |
Cavaignac, SM; De Voss, JJ; Ghasemi, Y; Hawkes, DB; Slessor, KE; Stok, JE | 1 |
Golinelli-Pimpaneau, B; Hamdane, D; Myllykallio, H; Skouloubris, S | 1 |
Andi, B; Bobyk, KD; Cook, PF; Kumar, VP; Thomas, LM; West, AH | 1 |
Bobik, TA; Cheng, S; Fan, C; Sinha, S | 1 |
Gontero, B; Halgand, F; Kaaki, W; Woudstra, M | 1 |
Deshpande, MV; Joshi, CV; Kapadnis, BP; Pathan, EK; Punekar, NS; Tupe, SG | 1 |
Kugimiya, A; Takamitsu, E | 1 |
Kim, HY; Quashie, PK; Shlaifer, I; Turnbull, JL | 1 |
Boreiko, S; de F P Melo, R; Iulek, J; Silber, AM; Silva, M | 1 |
Apfeld, J; Johnsen, SB; Stanley, JA | 1 |
Chailyan, SG; Danielyan, KE; Ginosyan, SV; Grabski, HV; Tiratsuyan, SG | 1 |
Eriksson, LA; Gholami, A; Mahdizadeh, SJ; Minai-Tehrani, D; Saenz-Mendez, P | 1 |
1 review(s) available for histidine and nad
Article | Year |
---|---|
Nuclear magnetic resonance studies of the dynamic aspects of molecular structure and interaction in biological systems.
Topics: Aspartate Carbamoyltransferase; Aspirin; Chymotrypsin; Histidine; Ligands; Macromolecular Substances; Magnetic Resonance Spectroscopy; Muramidase; NAD; Penicillin G; Peptides; Protein Binding; Protein Conformation; Protein Denaturation; Ribonucleases; Serum Albumin; Staphylococcus; Sulfonamides; Tryptophan; Valinomycin | 1972 |
161 other study(ies) available for histidine and nad
Article | Year |
---|---|
Properties of crystalline reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase from bovine adrenocortical mitochondria. II. Essential histidyl and cysteinyl residues at the NADPH binding site of NADPH-adrenodoxin reductase.
Topics: Adrenal Cortex; Adrenal Glands; Adrenodoxin; Animals; Binding Sites; Cattle; Cysteine; Diethyl Pyrocarbonate; Ferredoxin-NADP Reductase; Glutathione; Histidine; Hydrogen-Ion Concentration; Hydroxylamines; Light; Methylene Blue; Mitochondria; NAD; NADH, NADPH Oxidoreductases; NADP | 1976 |
A study of the ionic properties of the essential histidine residue of yeast alcohol dehydrogenase in complexes of the enzyme with its coenzymes and substrates.
Topics: Acetaldehyde; Alcohol Oxidoreductases; Coenzymes; Diethyl Pyrocarbonate; Ethanol; Histidine; Hydrogen; Hydrogen-Ion Concentration; Kinetics; NAD; Oxidation-Reduction; Saccharomyces cerevisiae | 1977 |
The role of an essential histidine residue of yeast alcohol dehydrogenase.
Topics: Alcohol Oxidoreductases; Binding Sites; Diethyl Pyrocarbonate; Histidine; Hydrogen-Ion Concentration; Kinetics; Mathematics; NAD; Photochemistry; Protein Binding; Saccharomyces cerevisiae; Spectrometry, Fluorescence | 1975 |
Comparison of octopine, histopine, lysopine, and octopinic acid synthesizing activities in sunflower crown gall tissues.
Topics: Amino Acids; Arginine; Histidine; Lysine; NAD; NADP; Ornithine; Plant Diseases; Pyruvates; Rhizobium | 1977 |
Studies of a reactive histidine of dyphosphopyridine nucleotide-linked isocitrate dehydrogenase from bovine heart.
Topics: Acetates; Amino Acids; Animals; Binding Sites; Cattle; Diethyl Pyrocarbonate; Histidine; Hydrogen-Ion Concentration; Isocitrate Dehydrogenase; Kinetics; Magnesium; Methylene Blue; Mitochondria, Heart; NAD; Rose Bengal | 1977 |
Malate dehydrogenase of the cytosol. Ionizations of the enzyme-reduced-coenzyme complex and a comparison with lactate dehydrogenase.
Topics: Benzimidazoles; Chemical Phenomena; Chemistry; Cytosol; Fluorometry; Histidine; Hydrogen-Ion Concentration; L-Lactate Dehydrogenase; Malate Dehydrogenase; NAD; Protein Binding | 1978 |
Use of the sulphite adduct of nicotinamide-adenine dinucleotide to study ionizations and the kinetics of lactate dehydrogenase and malate dehydrogenase.
Topics: Histidine; Hydrogen-Ion Concentration; Kinetics; L-Lactate Dehydrogenase; Malate Dehydrogenase; NAD; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Sulfites | 1978 |
Evidence for a histidine and a cysteine residue in the substrate-binding site of yeast alcohol dehydrogenase.
Topics: Acetamides; Alcohol Oxidoreductases; Binding Sites; Cysteine; Diethyl Pyrocarbonate; Dithionitrobenzoic Acid; Histidine; Molecular Weight; NAD; Yeasts | 1975 |
A study of the oxidation of butan-1-ol and propan-2-ol by nicotinamide-adenine dinucleotide catalysed by yeast alcohol dehydrogenase.
Topics: 1-Propanol; Alcohol Oxidoreductases; Butanols; Catalysis; Cysteine; Edetic Acid; Enzyme Activation; Histidine; Kinetics; Mathematics; NAD; Oxidation-Reduction; Temperature; Yeasts | 1975 |
Iodination of glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus.
Topics: Amino Acid Sequence; Apoenzymes; Electrophoresis; Geobacillus stearothermophilus; Glyceraldehyde-3-Phosphate Dehydrogenases; Histidine; Iodine; Monoiodotyrosine; NAD; Peptide Fragments; Protein Conformation; Spectrophotometry; Tyrosine | 1976 |
[The role of histidine residues of formate dehydrogenase from Bacterium sp. 1].
Topics: Aldehyde Oxidoreductases; Bacteria; Diethyl Pyrocarbonate; Dithionitrobenzoic Acid; Formates; Histidine; Kinetics; NAD | 1978 |
Chemical modification of bovine heart mitochondrial malate dehydrogenase. Selective modification of cysteine and histidine.
Topics: Amino Acids; Animals; Carbon Radioisotopes; Cattle; Cysteine; Ethylmaleimide; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Iodoacetates; Malate Dehydrogenase; Malates; Mitochondria, Muscle; Molecular Weight; Myocardium; NAD; Oxaloacetates; Urea | 1975 |
Characterization of two site-specifically mutated human dihydrolipoamide dehydrogenases (His-452----Gln and Glu-457----Gln).
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Cloning, Molecular; Dihydrolipoamide Dehydrogenase; Escherichia coli; Flavin-Adenine Dinucleotide; Genetic Vectors; Glutamates; Glutamic Acid; Glutamine; Histidine; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Oligodeoxyribonucleotides; Protein Conformation; Recombinant Proteins | 1992 |
Selectivity in the binding of NAD(P)+ analogues to NAD- and NADP-dependent pig heart isocitrate dehydrogenases. A nuclear magnetic resonance study.
Topics: Animals; Histidine; Isocitrate Dehydrogenase; Kinetics; Magnetic Resonance Spectroscopy; Molecular Conformation; Myocardium; NAD; NADP; Phosphorus; Swine | 1992 |
Pseudomonas aeruginosa exotoxin A interaction with eucaryotic elongation factor 2. Role of the His426 residue.
Topics: ADP Ribose Transferases; Antibodies, Monoclonal; Bacterial Toxins; Diethyl Pyrocarbonate; Exotoxins; Histidine; NAD; Peptide Elongation Factor 2; Peptide Elongation Factors; Poly(ADP-ribose) Polymerases; Protein Binding; Protein Conformation; Pseudomonas aeruginosa; Pseudomonas aeruginosa Exotoxin A; Structure-Activity Relationship; Virulence Factors | 1992 |
Structure-function analysis of exotoxin A proteins with mutations at histidine 426.
Topics: ADP Ribose Transferases; Bacterial Toxins; Base Sequence; Exotoxins; Histidine; Molecular Sequence Data; Mutation; NAD; Poly(ADP-ribose) Polymerases; Protein Conformation; Pseudomonas aeruginosa; Pseudomonas aeruginosa Exotoxin A; Structure-Activity Relationship; Virulence Factors | 1992 |
Involvement of histidine residues in catalytic activity of xanthine dehydrogenase from hen liver.
Topics: 2,6-Dichloroindophenol; Animals; Chickens; Diethyl Pyrocarbonate; Enzyme Activation; Female; Histidine; Kinetics; Liver; NAD; Oxidation-Reduction; Photochemistry; Structure-Activity Relationship; Xanthine; Xanthine Dehydrogenase; Xanthines | 1992 |
An essential histidine residue for the activity of UDPglucose 4-epimerase from Kluyveromyces fragilis.
Topics: Diethyl Pyrocarbonate; Enzyme Activation; Histidine; Kinetics; Kluyveromyces; NAD; Oxidation-Reduction; Spectrometry, Fluorescence; UDPglucose 4-Epimerase | 1992 |
Immunochemical analysis of Pseudomonas aeruginosa exotoxin A. Analysis of the His426 determinant.
Topics: ADP Ribose Transferases; Antibodies, Monoclonal; Bacterial Toxins; Enzyme-Linked Immunosorbent Assay; Epitopes; Exotoxins; Histidine; Hydrolysis; Immunohistochemistry; NAD; Poly(ADP-ribose) Polymerases; Precipitin Tests; Pseudomonas aeruginosa; Pseudomonas aeruginosa Exotoxin A; Urea; Virulence Factors | 1991 |
General base catalysis in a glutamine for histidine mutant at position 51 of human liver alcohol dehydrogenase.
Topics: Alcohol Dehydrogenase; Binding, Competitive; Catalysis; Decanoic Acids; Ethanol; Glutamine; Histidine; Humans; Isoenzymes; Kinetics; Liver; Mutagenesis; NAD; Trifluoroethanol | 1991 |
Singlet oxygen production from the reactions of ozone with biological molecules.
Topics: Antioxidants; Ascorbic Acid; Cysteine; Free Radicals; Histidine; Luminescent Measurements; Methionine; NAD; NADP; Ozone; Solvents; Uric Acid | 1991 |
Substitution of arginine for histidine-47 in the coenzyme binding site of yeast alcohol dehydrogenase I.
Topics: Alcohol Dehydrogenase; Arginine; Base Sequence; Binding Sites; DNA, Fungal; Histidine; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Mutation; NAD; Saccharomyces cerevisiae | 1990 |
Histidine-21 is involved in diphtheria toxin NAD+ binding.
Topics: Binding Sites; Diphtheria Toxin; Histidine; Hydrogen-Ion Concentration; NAD; Protein Conformation | 1990 |
Mutation in the phosphoribosylpyrophosphate synthetase gene (prs) that results in simultaneous requirements for purine and pyrimidine nucleosides, nicotinamide nucleotide, histidine, and tryptophan in Escherichia coli.
Topics: Escherichia coli; Histidine; Mutation; NAD; Phosphoribosyl Pyrophosphate; Phosphotransferases; Phosphotransferases (Alcohol Group Acceptor); Purine Nucleosides; Purine-Nucleoside Phosphorylase; Pyrimidine Nucleosides; Ribose-Phosphate Pyrophosphokinase; Tryptophan; Uridine Phosphorylase | 1988 |
Histidine 21 is at the NAD+ binding site of diphtheria toxin.
Topics: Adenine; Adenosine; Binding Sites; Diethyl Pyrocarbonate; Diphtheria Toxin; Formates; Histidine; Kinetics; NAD; Niacinamide; Peptide Fragments | 1989 |
Inactivation of 3 alpha-hydroxysteroid dehydrogenase by superoxide radicals. Modification of histidine and cysteine residues causes the conformational change.
Topics: 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific); 3-Hydroxysteroid Dehydrogenases; Amino Acids; Cysteine; Free Radicals; Histidine; NAD; Protein Conformation; Serum Albumin, Bovine; Spectrometry, Fluorescence; Superoxide Dismutase; Superoxides; Xanthine Oxidase | 1986 |
Chemical modification of 3 alpha,20 beta-hydroxysteroid dehydrogenase with diethyl pyrocarbonate. Evidence for an essential, highly reactive, lysyl residue.
Topics: Binding Sites; Binding, Competitive; Chemical Phenomena; Chemistry; Diethyl Pyrocarbonate; Formates; Histidine; Hydrogen-Ion Concentration; Hydroxylamines; Hydroxysteroid Dehydrogenases; Lysine; NAD; Progesterone; Protein Conformation; Streptomyces | 1987 |
Chemical modification of nitrate reductase from Amaranthus.
Topics: Binding Sites; Diethyl Pyrocarbonate; Histidine; Magnoliopsida; NAD; Nitrate Reductase; Nitrate Reductases; Plants | 1987 |
Characterization of an essential histidine residue in thermophilic malate dehydrogenase.
Topics: Diethyl Pyrocarbonate; Histidine; Hot Temperature; Hydrogen-Ion Concentration; Malate Dehydrogenase; NAD; Oxidation-Reduction; Photochemistry; Thermus | 1986 |
Diethylpyrocarbonate inactivation of NAD-malic enzyme from Ascaris suum.
Topics: Animals; Ascaris; Binding Sites; Chemical Phenomena; Chemistry; Diethyl Pyrocarbonate; Formates; Histidine; Hydrogen-Ion Concentration; Hydroxylamine; Hydroxylamines; Kinetics; Malate Dehydrogenase; Malates; NAD; Spectrometry, Fluorescence | 1985 |
New amino acids, and heterocyclic compounds participating in the Stickland reaction of Clostridium sticklandii.
Topics: Adenine; Alcohol Oxidoreductases; Amino Acids; Anaerobiosis; Chromatography, Thin Layer; Clostridium; Electron Transport; Fluorescence; Fluorometry; Formates; Glucosephosphate Dehydrogenase; Glutamate Dehydrogenase; Glutamates; Heterocyclic Compounds; Histidine; L-Lactate Dehydrogenase; Methods; NAD; NADP; Oxidation-Reduction; Pyrimidinones; Uric Acid; Xanthines | 1973 |
Stabilizing the alkali-generated fluorescent derivatives of NAD and NADP.
Topics: Chemical Phenomena; Chemistry; Drug Stability; Fluorescence; Fluorometry; Histidine; Hydrogen Peroxide; Hydrogen-Ion Concentration; Imidazoles; Light; NAD; NADP; Osmolar Concentration; Oxidation-Reduction; Sodium Hydroxide | 1974 |
[Specific incorporation of the coenzyme analogue (3-(3-bromoacetylpyridinio)propyl)-adenosine pyrophosphate into the alcohol dehydrogenase from yeast (author's transl)].
Topics: Alcohol Oxidoreductases; Binding Sites; Carbon Radioisotopes; Chromatography, Ion Exchange; Electrophoresis, Paper; Histidine; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; NAD; NADP; Oxidation-Reduction; Protein Binding; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Temperature | 1973 |
The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide phosphate oxidoreductase and histidine-2-oxoglutarate aminotransferase in the degradation of imidazol-5-yl-lactate by Pseudomonas acidovorans.
Topics: Histidine; Imidazoles; Ketoglutaric Acids; Lactates; Mutation; NAD; Oxidoreductases; Pseudomonas; Transaminases | 1969 |
Phosphorylation of protein in liver and kidney mitochondria of the rat.
Topics: Adenine Nucleotides; Animals; Arsenic; Depression, Chemical; Dinitrophenols; Guanine Nucleotides; Hexokinase; Histidine; Hydrogen-Ion Concentration; Kidney; Maleates; Malonates; Mitochondria; Mitochondria, Liver; Models, Biological; NAD; Oxidative Phosphorylation; Phosphates; Phosphorus Isotopes; Proteins; Rats; Serine; Stimulation, Chemical; Time Factors | 1968 |
Comparative structural properties of honeybee and rabbit alpha-glycerophosphate dehydrogenases.
Topics: Adenine Nucleotides; Alanine; Amino Acid Sequence; Amino Acids; Animals; Bees; Carboxypeptidases; Chemical Phenomena; Chemistry; Chromatography, Gel; Glycerolphosphate Dehydrogenase; Histidine; Hydrazines; Methionine; Molecular Weight; Muscles; NAD; Optical Rotatory Dispersion; Peptides; Protein Hydrolysates; Rabbits; Rats; Species Specificity; Time Factors; Trypsin | 1969 |
Effect of diazonium derivatives on myosin A adenosine triphosphatase. II. A possible conformational change induced by ATP.
Topics: Adenine Nucleotides; Adenosine Triphosphatases; Animals; Calcium; Depression, Chemical; Diazonium Compounds; Edetic Acid; Histidine; Hydrogen-Ion Concentration; In Vitro Techniques; Indicators and Reagents; Ions; Kinetics; Magnesium; Muscle Proteins; NAD; Potassium; Rabbits; Time Factors | 1969 |
Glutamine synthetase of Neurospora crassa. Inactivation by urea and protection by some substrates and allosteric effectors.
Topics: Centrifugation, Density Gradient; Chemical Phenomena; Chemistry; Chloromercuribenzoates; Glutamates; Glutamine; Glycine; Histidine; Ligases; Magnesium; Molecular Weight; NAD; Neurospora; ortho-Aminobenzoates; Sulfhydryl Compounds; Urea | 1969 |
Structural studies on the active center of alpha-glycerolphosphate dehydrogenase.
Topics: Animals; Azo Compounds; Azoles; Binding Sites; Chemical Phenomena; Chemistry; Computers; Darkness; Glycerolphosphate Dehydrogenase; Histidine; Ketones; Kinetics; Light; Muscles; NAD; Phosphoric Acids; Rabbits; Radiation Effects; Rose Bengal; Spectrophotometry; Ultraviolet Rays | 1970 |
An essential histidine in the catalytic activities of 3-phosphoglyceraldehyde dehydrogenase.
Topics: Amino Acid Sequence; Amino Acids; Animals; Darkness; Esterases; Glyceraldehyde-3-Phosphate Dehydrogenases; Histidine; Kinetics; Light; Muscles; NAD; Oxidation-Reduction; Oxidoreductases; Peptides; Phenylacetates; Rabbits; Radiation Effects; Rose Bengal; Spectrophotometry | 1970 |
Effect of diethylpyrocarbonate on the conformation and enzymic activity of d-glyceraldehyde-3-phosphate dehydrogenase.
Topics: Animals; Carbonates; Charcoal; Chemical Phenomena; Chemistry; Chromatography, Gel; Enzyme Activation; Fluorometry; Glucosephosphate Dehydrogenase; Histidine; Kinetics; Mercaptoethanol; Muscles; NAD; Peptides; Phosphates; Protein Denaturation; Swine | 1969 |
Relationship of a membrane-bound D-(-)-lactic dehydrogenase to amino acid transport in isolated bacterial membrane preparations.
Topics: Acetates; Amino Acids; Biological Transport, Active; Butyrates; Carbon Isotopes; Citrates; Escherichia coli; Formates; Fumarates; Glyceric Acids; Hexosephosphates; Histidine; Hydroxybutyrates; Isoleucine; Ketoglutaric Acids; L-Lactate Dehydrogenase; Lactates; Leucine; Malates; Membranes; NAD; Oxaloacetates; Phenylalanine; Proline; Pyruvates; Stereoisomerism; Succinates; Thyroxine | 1970 |
The kinetics of the reactions catalyzed by D-glyceraldehyde-3-phosphate dehydrogenase. 3. The pH dependence of apparent michaelis constants and maximum velocity.
Topics: Animals; Chemical Phenomena; Chemistry; Cysteine; Glyceraldehyde-3-Phosphate Dehydrogenases; Glycerophosphates; Histidine; Hydrogen-Ion Concentration; Kinetics; Mathematics; Muscles; NAD; Swine | 1967 |
Alkylation studies on a reactive histidine in pig heart malate dehydrogenase.
Topics: Adenine Nucleotides; Alkylation; Animals; Bromine; Histidine; Hydrogen-Ion Concentration; Iodoacetates; Kinetics; Malate Dehydrogenase; Malates; Mitochondria, Muscle; Myocardium; NAD; Niacinamide; Oxaloacetates; Propionates; Swine | 1970 |
[Assignment of an essential histidine residue to the substrate binding site of lactate dehydrogenase].
Topics: Amino Acid Sequence; Animals; Binding Sites; Carbon Isotopes; Histidine; Kinetics; L-Lactate Dehydrogenase; Myocardium; NAD; Niacinamide; Nucleotides; Pyruvates; Swine | 1971 |
Properties of a fused protein formed by genetic manipulation. Histidinol dehydrogenase-imidazolylacetol phosphate: L-glutamate aminotransferase.
Topics: Alcohol Oxidoreductases; Amino Alcohols; Bacterial Proteins; Centrifugation, Density Gradient; Chemical Phenomena; Chemistry; Drug Stability; Electrophoresis; Genes; Glutamates; Histidine; Hot Temperature; Imidazoles; Ketoglutaric Acids; Kinetics; Molecular Weight; Mutation; NAD; Operon; Peptides; Polymers; Salmonella typhimurium; Spectrophotometry; Transaminases; Trypsin | 1971 |
Regulation of glutamate dehydrogenase by histidine.
Topics: Acetates; Adenine Nucleotides; Amino Acids; Animals; Binding Sites; Cattle; Chemical Phenomena; Chemistry; Dipeptides; Enzyme Activation; Fluorescence; Glutamate Dehydrogenase; Histidine; Kinetics; Leucine; Liver; Methylation; NAD; Urea; Valerates | 1971 |
A new type of histidine regulatory mutant in Escherichia coli.
Topics: Alcohol Oxidoreductases; Carbon Isotopes; Cell-Free System; Culture Media; Depression, Chemical; Enzyme Repression; Escherichia coli; Genetics, Microbial; Histidine; Leucine; Mutation; NAD; Operon; RNA, Bacterial; RNA, Transfer; Salmonella typhimurium; Species Specificity; Stimulation, Chemical; Temperature | 1971 |
The inhibition of glutamate dehydrogenase by L-serine O-sulphate and related compounds and by photo-oxidation in the presence of Rose Bengal.
Topics: Adenosine Diphosphate; Amino Acids; Dialysis; Enzyme Activation; Esters; Glutamate Dehydrogenase; Glutamates; Guanosine Triphosphate; Histidine; Hydrogen-Ion Concentration; NAD; Photochemistry; Rose Bengal; Serine; Time Factors | 1971 |
Characterization of porcine malate dehydrogenase. I. An active center peptide.
Topics: Acetamides; Amino Acid Sequence; Animals; Binding Sites; Carbon Isotopes; Carboxypeptidases; Chromatography, Ion Exchange; Chromatography, Thin Layer; Cysteine; Dansyl Compounds; Glycine; Histidine; Iodoacetates; Kinetics; Malate Dehydrogenase; Methionine; Mitochondria, Muscle; Myocardium; NAD; Peptides; Pronase; Serine; Swine; Threonine | 1971 |
The effects of pH and temperature on hydrogen transfer in the liver alcohol dehydrogenase mechanism.
Topics: Alcohol Oxidoreductases; Catalysis; Ethanol; Histidine; Hydrogen-Ion Concentration; Kinetics; Liver; NAD; Spectrophotometry; Temperature; Thermodynamics; Ultraviolet Rays | 1972 |
Affinity labeling of steroid binding sites. Synthesis of 16 -bromoacetoxyprogesterone and its use for affinity labeling of 20 -hydroxysteroid dehydrogenase.
Topics: Acetates; Alkylation; Amino Acids; Binding Sites; Bromine; Cortisone; Crystallization; Drug Stability; Esters; Histidine; Hydroxyprogesterones; Hydroxysteroid Dehydrogenases; Isotope Labeling; Mercaptoethanol; Models, Chemical; Models, Structural; NAD; Oxidation-Reduction; Progesterone; Streptomyces; Structure-Activity Relationship; Tritium | 1972 |
Antigen-free medium for cultivation of Haemophilus influenzae, AFH-medium.
Topics: Antigens; Antigens, Bacterial; Chromatography, Gel; Culture Media; Densitometry; Glucose; Haemophilus influenzae; Heme; Histidine; Hydrogen-Ion Concentration; Molecular Weight; NAD; Phosphates; Potassium; Sodium Chloride; Spectrophotometry | 1972 |
Reaction of glyceraldehyde-3-phosphate dehydrogenase with dibromoacetone.
Topics: Acetone; Alkylation; Amino Acids; Ammonium Sulfate; Animals; Benzoates; Binding Sites; Borohydrides; Bromine; Carbon Isotopes; Chemical Phenomena; Chemistry; Cysteine; Disulfides; Formates; Glyceraldehyde-3-Phosphate Dehydrogenases; Histidine; Hydrogen-Ion Concentration; Iodoacetates; Kinetics; Mass Spectrometry; Models, Chemical; Muscles; NAD; Nitro Compounds; Oxidation-Reduction; Rabbits | 1972 |
The histidines in liver alcohol dehydrogenase. Chemical modification with diethylpyrocarbonate.
Topics: Alcohol Oxidoreductases; Amides; Animals; Binding Sites; Butyrates; Carbonates; Chemical Phenomena; Chemistry; Dicarboxylic Acids; Enzyme Activation; Histidine; Horses; Liver; NAD; Protein Conformation | 1972 |
The role of histidine residues in glutamate dehydrogenase.
Topics: Acylation; Adenosine Diphosphate; Anhydrides; Animals; Cattle; Formates; Glutamate Dehydrogenase; Glutamates; Guanosine Triphosphate; Histidine; Hydrogen-Ion Concentration; NAD; Oxidation-Reduction; Photochemistry; Rose Bengal | 1972 |
Effects of photooxidation of histidine-38 on the various catalytic activities of glyceraldehyde-3-phosphate dehydrogenase.
Topics: Acetates; Acetylation; Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Sequence; Animals; Arsenic; Autoradiography; Binding Sites; Carbon Isotopes; Drug Stability; Electrophoresis, Paper; Glyceraldehyde; Glyceraldehyde-3-Phosphate Dehydrogenases; Histidine; Hydrogen-Ion Concentration; Muscles; NAD; Nitrobenzenes; Oxidation-Reduction; Phosphoric Acids; Photochemistry; Rabbits; Rose Bengal | 1973 |
Effects of photooxidation of histidine-38 on the acetylphosphatase activity of glyceraldehyde-3-phosphate dehydrogenase.
Topics: Acetates; Adenosine Diphosphate; Amino Acid Sequence; Animals; Apoproteins; Arsenic; Binding Sites; Catalysis; Cysteine; Drug Stability; Esterases; Glyceraldehyde-3-Phosphate Dehydrogenases; Histidine; Imidazoles; Muscles; NAD; Oxidation-Reduction; Phosphoric Monoester Hydrolases; Photochemistry; Rabbits; Rose Bengal | 1973 |
Studies of glutamate dehydrogenase. Characterization of histidine residues involved in the activity and association. Photoactivated labelling with pyridoxal 5'-phosphate.
Topics: Adenosine Diphosphate; Amino Acids; Binding Sites; Carbonates; Diphosphates; Enzyme Activation; Glutamate Dehydrogenase; Guanosine Triphosphate; Histidine; Imidazoles; Light; Lysine; NAD; Photochemistry; Protein Binding; Protein Conformation; Pyridoxal Phosphate; Schiff Bases; Spectrophotometry, Ultraviolet; Tritium | 1973 |
Comparative transport activity of intact cells, membrane vesicles, and mesosomes of Bacillus licheniformis.
Topics: Alanine; Amino Acids; Aspartic Acid; Bacillus; Biological Transport, Active; Carbon Isotopes; Cell Fractionation; Cell Membrane; Cell Membrane Permeability; Centrifugation, Density Gradient; Chromatography, Paper; Culture Media; Glutamates; Histidine; Inclusion Bodies; Light; Lysine; NAD; Sodium; Stereoisomerism; Succinates; Vitamin K | 1973 |
Functional groups in the catalysis and regulation of Escherichia coli citrate synthase.
Topics: Catalysis; Citrate (si)-Synthase; Citric Acid Cycle; Cysteine; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Methylene Blue; NAD; Oxidation-Reduction; Oxo-Acid-Lyases | 1972 |
The reaction of a histidine residue in glutamate dehydrogenase with diethyl pyrocarbonate.
Topics: Adenosine Diphosphate; Animals; Binding Sites; Cattle; Chemical Phenomena; Chemistry; Enzyme Activation; Esters; Formates; Glutamate Dehydrogenase; Histidine; Kinetics; Liver; NAD; Protein Binding; Spectrophotometry, Ultraviolet; Time Factors | 1973 |
Ionic properties of an essential histidine residue in pig heart lactate dehydrogenase.
Topics: Acylation; Animals; Binding Sites; Esters; Formates; Histidine; Hydrogen-Ion Concentration; Kinetics; L-Lactate Dehydrogenase; Models, Chemical; Myocardium; NAD; Protein Binding; Protein Denaturation; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Swine; Time Factors | 1973 |
The use of ternary complexes to study ionizations and isomerizations during catalysis by lactate dehydrogenase.
Topics: Amino Acids; Animals; Binding Sites; Chemical Phenomena; Chemistry; Glyoxylates; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Isomerism; Kinetics; L-Lactate Dehydrogenase; Muscles; Myocardium; NAD; Nitro Compounds; Phenylpyruvic Acids; Protein Binding; Spectrometry, Fluorescence; Swine; Time Factors | 1973 |
An operon for histidine biosynthesis in Streptomyces coelicolor. II. Biochemical evidence.
Topics: Alcohol Oxidoreductases; Allosteric Regulation; Amino Alcohols; Enzyme Induction; Enzyme Repression; Glycerophosphates; Histidine; Hydro-Lyases; Imidazoles; NAD; Operon; Phosphates; Phosphoric Monoester Hydrolases; Streptomyces | 1973 |
Arabinose (fucose) dehydrogenase from pig liver. I. Isolation and characterization.
Topics: Alcohol Oxidoreductases; Animals; Arabinose; Binding Sites; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Fucose; Glucose Oxidase; Histidine; Hydrogen-Ion Concentration; Kinetics; Liver; Molecular Weight; NAD; Osmolar Concentration; Protein Binding; Swine | 1973 |
Some properties of a homocarnosine-carnosine synthetase isolated from rat brain.
Topics: Adenosine Diphosphate; Adenosine Monophosphate; Adenosine Triphosphate; Alanine; Aminobutyrates; Ammonium Sulfate; Animals; Brain; Carbon Radioisotopes; Chromatography; Chromatography, Paper; Dialysis; Dipeptides; Diphosphates; Electrophoresis, Paper; Female; Histidine; Hydrogen-Ion Concentration; NAD; Nerve Tissue Proteins; Peptide Synthases; Peptides; Rats | 1973 |
Functional groups in the activity and regulation of Escherichia coli citrate synthase.
Topics: Amino Acids; Benzoates; Benzyl Compounds; Binding Sites; Citrate (si)-Synthase; Cysteine; Densitometry; Disulfides; Escherichia coli; Esters; Formates; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Ketoglutaric Acids; Kinetics; Methylene Blue; Molecular Weight; NAD; Nitro Compounds; Nitrobenzenes; Oxidation-Reduction; Oxo-Acid-Lyases; Phenols; Photochemistry; Rose Bengal; Tryptophan | 1973 |
The degradation of L-histidine in the rat. The formation of imidazolylpyruvate, imidazolyl-lactate and imidazolylpropionate.
Topics: Alcohol Oxidoreductases; Animals; Chromatography, DEAE-Cellulose; Histidine; Imidazoles; Intestines; Ketoglutaric Acids; L-Lactate Dehydrogenase; Lactates; Mitochondria, Liver; Molecular Weight; NAD; Phenylalanine; Propionates; Pyruvates; Rats; Transaminases; Tyrosine | 1973 |
Dihydroxyacetone sulfate as substrate analogue for alpha-glycerol phosphate dehydrogenase.
Topics: Acetone; Animals; Benzoates; Chromatography, DEAE-Cellulose; Chromatography, Ion Exchange; Disulfides; Dithiothreitol; Electrophoresis, Disc; Glycerolphosphate Dehydrogenase; Histidine; Hydrogen-Ion Concentration; Kinetics; Muscles; NAD; Nitro Compounds; Organophosphorus Compounds; Oxidation-Reduction; Rabbits; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Sulfuric Acids; Trioses | 1974 |
Characterization of porcine malate dehydrogenase. II. Amino acid sequence of a peptide containing the active center histidine residue.
Topics: Amino Acid Sequence; Amino Acids; Animals; Binding Sites; Carbon Radioisotopes; Carboxypeptidases; Chromatography, Gel; Chromatography, Ion Exchange; Chromatography, Paper; Chromatography, Thin Layer; Dansyl Compounds; Electrophoresis, Paper; Histidine; Iodoacetates; Kinetics; Malate Dehydrogenase; Myocardium; NAD; Oxidation-Reduction; Peptide Fragments; Protein Binding; Swine; Time Factors; Trypsin | 1974 |
Histidine residues and the enzyme activity of pig heart supernatant malate dehydrogenase.
Topics: Animals; Binding Sites; Ethyl Ethers; Formates; Histidine; Hydrogen-Ion Concentration; Kinetics; Malate Dehydrogenase; Molecular Conformation; Myocardium; NAD; Oxaloacetates; Protein Binding; Swine; Tartronates | 1974 |
[Recent data on D(minus) beta-hydroxybutyrate dehydrogenase of rat liver mitochondria].
Topics: Acetoacetates; Acids; Animals; Binding Sites; Binding, Competitive; Histidine; Hydroxybutyrate Dehydrogenase; Hydroxybutyrates; Kinetics; Malonates; Mercaptoethanol; Mitochondria, Liver; NAD; Oxaloacetates; Rats; Succinates; Sulfur | 1974 |
Glucose dehydrogenase from pig liver. I. Isolation and purification.
Topics: Alcohol Oxidoreductases; Animals; Binding Sites; Chromatography, Gel; Crystallization; Glucose; Hexosephosphates; Histidine; Hydrogen-Ion Concentration; Kinetics; Liver; Molecular Weight; NAD; NADP; Osmolar Concentration; Quaternary Ammonium Compounds; Sulfates; Swine; Temperature | 1970 |
Investigation of the pH dependence of proton uptake by porcine heart mitochondrial malate dehydrogenase upon binding of NADH.
Topics: Animals; Binding Sites; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Malate Dehydrogenase; Mitochondria, Heart; NAD; Protein Binding; Protons; Swine | 1980 |
Involvement of histidine residues in the activity of horse liver alcohol dehydrogenase.
Topics: Alcohol Dehydrogenase; Alcohol Oxidoreductases; Animals; Apoenzymes; Binding Sites; Diethyl Pyrocarbonate; Histidine; Horses; Kinetics; Liver; NAD; Protein Conformation; X-Ray Diffraction | 1983 |
Diphthamide in elongation factor 2: ADP-ribosylation, purification, and properties.
Topics: Adenosine Diphosphate Ribose; Diphtheria Toxin; Histidine; NAD; Nucleoside Diphosphate Sugars; Peptide Elongation Factor 2; Peptide Elongation Factors; Phosphorus Radioisotopes; Protein Processing, Post-Translational; Radioisotope Dilution Technique | 1984 |
Inhibition of mitochondrial NADH:ubiquinone oxidoreductase by ethoxyformic anhydride.
Topics: Animals; Cattle; Diethyl Pyrocarbonate; Electron Transport; Formates; Histidine; Hydroxylamine; Hydroxylamines; Kinetics; Meperidine; Mitochondria, Heart; NAD; NAD(P)H Dehydrogenase (Quinone); NADH, NADPH Oxidoreductases; Quinone Reductases; Tyrosine | 1984 |
Evidence for an essential histidine residue in S-adenosylhomocysteinase from rat liver.
Topics: Adenosine; Adenosylhomocysteinase; Animals; Chromatography, Gel; Diethyl Pyrocarbonate; Histidine; Hydrolases; Kinetics; Liver; NAD; Rats; Spectrometry, Fluorescence | 1983 |
Modification of aspartate before its condensation with dihydroxyacetone phosphate during quinolinic acid formation in Escherichia coli.
Topics: Aspartic Acid; Cell-Free System; Dihydroxyacetone Phosphate; Escherichia coli; Fructosediphosphates; Histidine; Mutation; NAD; Proline; Pyridines; Quinolinic Acids; Trioses | 1980 |
Patterns of product inhibition of a bifunctional dehydrogenase; L-histidinol:NAD+ oxidoreductase.
Topics: Alcohol Oxidoreductases; Histidine; Histidinol; Kinetics; Mathematics; NAD; Oxidation-Reduction; Salmonella typhimurium | 1981 |
Roles of histidine-194, aspartate-163, and a glycine-rich sequence of NAD(P)H:quinone oxidoreductase in the interaction with nicotinamide coenzymes.
Topics: Animals; Aspartic Acid; Base Sequence; Binding Sites; Consensus Sequence; DNA Primers; Histidine; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; NAD(P)H Dehydrogenase (Quinone); NADP; Oxidation-Reduction; Rats; Structure-Activity Relationship; Vitamin K | 1995 |
Purification and characterization of the Comamonas testosteroni B-356 biphenyl dioxygenase components.
Topics: Amino Acid Sequence; Base Sequence; Biphenyl Compounds; Electron Transport; Enzyme Inhibitors; Enzyme Stability; Escherichia coli; Ferredoxin-NADP Reductase; Ferredoxins; Flavin-Adenine Dinucleotide; Gram-Negative Aerobic Bacteria; Histidine; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Molecular Sequence Data; Molecular Weight; NAD; Oxidation-Reduction; Oxygenases; Peptides; Recombinant Fusion Proteins; Substrate Specificity; Temperature | 1995 |
Mechanistic studies on malate dehydrogenase from Escherichia coli.
Topics: Binding Sites; Deuterium; Diethyl Pyrocarbonate; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Iodoacetates; Iodoacetic Acid; Kinetics; Malate Dehydrogenase; NAD | 1995 |
Characterization of the interaction of NADH with proton pumping E. coli transhydrogenase reconstituted in the absence and in the presence of bacteriorhodopsin.
Topics: Bacteriorhodopsins; Binding Sites; Escherichia coli; Histidine; NAD; NADP; NADP Transhydrogenases | 1995 |
His273 of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8 is involved in the coenzyme binding.
Topics: 3-Isopropylmalate Dehydrogenase; Alcohol Oxidoreductases; Amino Acid Sequence; Bacteria; Base Sequence; Binding Sites; Histidine; Kinetics; Macromolecular Substances; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Oligodeoxyribonucleotides; Recombinant Proteins; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Thermus thermophilus | 1995 |
Common features of the NAD-binding and catalytic site of ADP-ribosylating toxins.
Topics: Adenosine Diphosphate Ribose; ADP Ribose Transferases; Amino Acid Sequence; Arginine; Bacillus; Bacterial Toxins; Binding Sites; Catalysis; Cholera Toxin; Computer Graphics; Conserved Sequence; Diphtheria Toxin; Enterotoxins; Escherichia coli; Escherichia coli Proteins; Exotoxins; Histidine; Models, Molecular; Molecular Sequence Data; NAD; Pertussis Toxin; Protein Structure, Secondary; Pseudomonas aeruginosa; Pseudomonas aeruginosa Exotoxin A; Sequence Homology, Amino Acid; Virulence Factors; Virulence Factors, Bordetella | 1994 |
Identification of a second active site residue in Escherichia coli L-threonine dehydrogenase: methylation of histidine-90 with methyl p-nitrobenzenesulfonate.
Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Benzenesulfonates; Binding Sites; Escherichia coli; Histidine; Methylation; Models, Chemical; Molecular Sequence Data; NAD; Oxidation-Reduction; Peptide Mapping; Sequence Homology, Amino Acid; Stereoisomerism; Threonine | 1995 |
The effect of replacing the conserved active-site residues His-264, Asp-312 and Arg-314 on the binding and catalytic properties of Escherichia coli citrate synthase.
Topics: Anilino Naphthalenesulfonates; Arginine; Aspartic Acid; Base Sequence; Binding Sites; Catalysis; Citrate (si)-Synthase; Dithionitrobenzoic Acid; Escherichia coli; Histidine; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Protein Conformation; Structure-Activity Relationship | 1994 |
Steady-state kinetics of cabbage histidinol dehydrogenase.
Topics: Alcohol Oxidoreductases; Brassica; Histidine; Histidinol; Kinetics; Models, Chemical; NAD; Recombinant Proteins | 1994 |
Role of histidine 35 of the S1 subunit of pertussis toxin in the ADP-ribosylation of transducin.
Topics: Adenosine Diphosphate Ribose; Amino Acid Sequence; Base Sequence; Binding Sites; Cloning, Molecular; Escherichia coli; Histidine; Kinetics; Macromolecular Substances; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Oligodeoxyribonucleotides; Pertussis Toxin; Point Mutation; Poly(ADP-ribose) Polymerases; Recombinant Proteins; Transducin; Virulence Factors, Bordetella | 1994 |
Active-site mutations of the diphtheria toxin catalytic domain: role of histidine-21 in nicotinamide adenine dinucleotide binding and ADP-ribosylation of elongation factor 2.
Topics: Adenosine Diphosphate Ribose; Amino Acid Sequence; Binding Sites; Calorimetry; Cloning, Molecular; Diphtheria Toxin; Escherichia coli; Genes, Synthetic; Histidine; Hydrogen Bonding; Kinetics; Mutagenesis, Insertional; NAD; NAD+ Nucleosidase; Peptide Elongation Factor 2; Peptide Elongation Factors; Poly(ADP-ribose) Polymerases; Recombinant Fusion Proteins; Recombinant Proteins; Restriction Mapping | 1994 |
Structures of horse liver alcohol dehydrogenase complexed with NAD+ and substituted benzyl alcohols.
Topics: Alcohol Dehydrogenase; Amino Acid Sequence; Animals; Benzyl Alcohols; Binding Sites; Crystallography, X-Ray; Fourier Analysis; Histidine; Horses; Hydrogen Bonding; Liver; Macromolecular Substances; NAD; Protein Conformation; Thermodynamics | 1994 |
Histidinol dehydrogenase loses its catalytic function through the mutation of His261-->Asn due to its inability to ligate the essential Zn.
Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Asparagine; Base Sequence; Brassica; Catalysis; Histidine; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; NAD; Recombinant Proteins; Zinc | 1994 |
Zinc ions bound to chimeric His4/lactate dehydrogenase facilitate decarboxylation of oxaloacetate.
Topics: Amino Acid Sequence; Base Sequence; Geobacillus stearothermophilus; Histidine; L-Lactate Dehydrogenase; Lactates; Lactic Acid; Metalloproteins; Molecular Sequence Data; NAD; Oxaloacetates; Peptides; Recombinant Fusion Proteins; Zinc | 1993 |
Active site phosphorylation of enzyme I of the bacterial phosphotransferase system by an ATP-dependent kinase.
Topics: Binding Sites; Chromatography, Affinity; Chromatography, Gel; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Escherichia coli; Histidine; Kinetics; Molecular Weight; NAD; NADP; Phosphoenolpyruvate Sugar Phosphotransferase System; Phosphorylation; Potassium | 1996 |
Construction and characterization of a deletion mutant of gpd2 that encodes an isozyme of NADH-dependent glycerol-3-phosphate dehydrogenase in fission yeast.
Topics: DNA, Fungal; Gene Expression Regulation, Enzymologic; Glycerol; Glycerolphosphate Dehydrogenase; Histidine; Isoenzymes; Lysine; Mutation; NAD; Osmolar Concentration; Phenotype; Schizosaccharomyces | 1996 |
Magnetic and optical properties of copper-substituted alcohol dehydrogenase: a bisthiolate copper (II) complex.
Topics: Alcohol Dehydrogenase; Animals; Circular Dichroism; Copper; Cysteine; Electron Spin Resonance Spectroscopy; Histidine; Horses; Ligands; Liver; Metalloproteins; Models, Chemical; NAD; Normal Distribution; Pyrazoles; Water | 1996 |
Histidine residues in rabbit liver microsomal cytochrome P-450 2B4 control electron transfer from NADPH-cytochrome P-450 reductase and cytochrome b5.
Topics: Acylation; Animals; Aryl Hydrocarbon Hydroxylases; Binding Sites; Cytochrome P-450 Enzyme System; Cytochromes b5; Diethyl Pyrocarbonate; Electron Transport; Histidine; In Vitro Techniques; Kinetics; Male; Microsomes, Liver; Molecular Structure; NAD; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Rabbits; Steroid Hydroxylases | 1996 |
The role of conserved histidine residues in the pyridine nucleotide transhydrogenase of Escherichia coli.
Topics: Amino Acid Sequence; Binding Sites; Catalysis; Conserved Sequence; Diethyl Pyrocarbonate; Enzyme Inhibitors; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; NAD; NADP Transhydrogenases; Point Mutation; Protons; Substrate Specificity; Trypsin | 1996 |
Cloning, nucleotide sequence and expression of a mannitol dehydrogenase gene from Pseudomonas fluorescens DSM 50106 in Escherichia coli.
Topics: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Chromatography, Affinity; Escherichia coli; Genes, Bacterial; Genomic Library; Histidine; Mannitol Dehydrogenases; Molecular Sequence Data; NAD; NADP; Peptides; Protein Engineering; Pseudomonas fluorescens; Recombinant Proteins; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Substrate Specificity | 1997 |
Protein-protein interaction of the human poly(ADP-ribosyl)transferase depends on the functional state of the enzyme.
Topics: Adenosine Diphosphate Ribose; beta-Galactosidase; Binding Sites; DNA; Gene Deletion; HeLa Cells; Histidine; Histones; Humans; NAD; Poly(ADP-ribose) Polymerases; Protein Binding; Recombinant Fusion Proteins; Sodium Chloride; Zinc Fingers | 1997 |
Fourier transform infrared spectroscopic studies of proton transfer processes and the dissociation of Zn2+-bound water in alcohol dehydrogenases.
Topics: Adenine; Adenosine Diphosphate Ribose; Alcohol Dehydrogenase; Animals; Histidine; Horses; Hydrogen Bonding; Liver; NAD; Protons; Saccharomyces cerevisiae; Spectroscopy, Fourier Transform Infrared; Trifluoroethanol; Water; Zinc | 1997 |
delta-Aminolevulinate dehydratase inhibition by ascorbic acid is mediated by an oxidation system existing in the hepatic supernatant.
Topics: Animals; Ascorbic Acid; Binding Sites; Cysteine; Dithiothreitol; Edetic Acid; Enzyme Inhibitors; Free Radical Scavengers; Glutathione; Histidine; Liver; Mannitol; NAD; Oxidation-Reduction; Porphobilinogen Synthase; Rats; Sulfhydryl Compounds; Superoxide Dismutase | 1998 |
Site-directed mutagenesis identifies amino acid residues associated with the dehydrogenase and isomerase activities of human type I (placental) 3beta-hydroxysteroid dehydrogenase/isomerase.
Topics: Amino Acid Sequence; Histidine; Humans; Kinetics; Molecular Sequence Data; Molecular Weight; Multienzyme Complexes; Mutagenesis, Site-Directed; NAD; Point Mutation; Progesterone Reductase; Recombinant Proteins; Steroid Isomerases; Tyrosine | 1998 |
Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD.
Topics: Amino Acid Sequence; Animals; Aspartic Acid; Binding Sites; Crystallography, X-Ray; Cytoplasm; Histidine; Malate Dehydrogenase; Malonates; Molecular Sequence Data; NAD; Protein Conformation; Protein Structure, Secondary; Substrate Specificity; Swine | 1999 |
Role of ground and excited singlet state oxygen in the red light-induced stimulation of Escherichia coli cell growth.
Topics: Azides; Deuterium Oxide; Escherichia coli; Histidine; Lasers; Light; NAD; NADH Dehydrogenase; Oxygen; Photobiology; Singlet Oxygen; Time Factors; Tryptophan; Water | 1999 |
Control of coenzyme binding to horse liver alcohol dehydrogenase.
Topics: Alcohol Dehydrogenase; Animals; Arginine; Coenzymes; Computer Simulation; Glutamine; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Liver; Lysine; Mutagenesis, Site-Directed; NAD; Protein Binding | 1999 |
Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis.
Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Catalysis; Circular Dichroism; Deuterium; Histidine; Kinetics; Lysine; Mutagenesis, Site-Directed; Mycobacterium tuberculosis; NAD; Oxidoreductases; Peptide Fragments; Recombinant Proteins; Solvents; Tyrosine | 1999 |
Roles of his205, his296, his303 and Asp259 in catalysis by NAD+-specific D-lactate dehydrogenase.
Topics: Amino Acid Substitution; Aspartic Acid; Bacterial Proteins; Binding Sites; Catalysis; Histidine; Hydrogen-Ion Concentration; Kinetics; L-Lactate Dehydrogenase; Lactate Dehydrogenases; Lactobacillus; Models, Molecular; Mutagenesis, Site-Directed; NAD; Point Mutation; Recombinant Fusion Proteins; Structure-Activity Relationship | 2000 |
Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: properties of the soluble W676H and W676A mutant reductases.
Topics: Alanine; Binding Sites; Catalysis; Cytochrome c Group; Enzyme Activation; Flavin-Adenine Dinucleotide; Histidine; Humans; Kinetics; Mutagenesis, Site-Directed; NAD; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Structure, Tertiary; Recombinant Proteins; Solubility; Spectrometry, Fluorescence; Thermodynamics; Tryptophan | 2000 |
Characterization of mutants of beta histidine91, beta aspartate213, and beta asparagine222, possible components of the energy transduction pathway of the proton-translocating pyridine nucleotide transhydrogenase of Escherichia coli.
Topics: Amino Acid Sequence; Amino Acid Substitution; Asparagine; Aspartic Acid; Binding Sites; Energy Metabolism; Escherichia coli; Histidine; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protein Conformation | 2001 |
Critical residues for the specificity of cofactors and substrates in human estrogenic 17beta-hydroxysteroid dehydrogenase 1: variants designed from the three-dimensional structure of the enzyme.
Topics: 17-Hydroxysteroid Dehydrogenases; Animals; Binding Sites; Catalytic Domain; Cells, Cultured; Histidine; Humans; Leucine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; NAD; NADP; Protein Conformation; Serine | 2001 |
Conserved residues in domain Ia are required for the reaction of Escherichia coli DNA ligase with NAD+.
Topics: Alanine; Amino Acid Sequence; Aspartic Acid; DNA Ligases; Dose-Response Relationship, Drug; Escherichia coli; Gene Deletion; Histidine; Kinetics; Ligands; Models, Biological; Molecular Sequence Data; Mutation; NAD; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Structure-Activity Relationship; Time Factors; Tyrosine | 2002 |
Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase.
Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Binding Sites; Catalysis; Cloning, Molecular; Dimerization; Escherichia coli; Histidine; Models, Chemical; Models, Molecular; Molecular Sequence Data; NAD; Protein Binding; Protein Folding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; X-Ray Diffraction; Zinc | 2002 |
NAD-dependent inhibition of the NAD-glycohydrolase activity in A549 cells.
Topics: ADP-ribosyl Cyclase; Apoptosis; Arginine; Cell Membrane; Epithelial Cells; Flow Cytometry; Histidine; Humans; Hydrolysis; Lung; NAD; NAD+ Nucleosidase; Propidium; Protein Transport | 2002 |
Identification of the first fungal NADP-GAPDH from Kluyveromyces lactis.
Topics: Amino Acid Sequence; Blotting, Northern; Cloning, Molecular; Galactose; Gene Library; Glucose; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenase (NADP+)(Phosphorylating); Histidine; Kluyveromyces; Mitochondria; Molecular Sequence Data; Mutation; NAD; NADP; Phenotype; Phosphoglycerate Kinase; Plasmids; RNA, Messenger; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Transcription, Genetic; Xylose | 2002 |
Mutational, structural, and kinetic studies of the ATP-binding site of Methanobacterium thermoautotrophicum nicotinamide mononucleotide adenylyltransferase.
Topics: Adenosine Triphosphate; Alanine; Amino Acid Motifs; Arginine; Binding Sites; Catalysis; Crystallography, X-Ray; DNA Mutational Analysis; Histidine; Kinetics; Methanobacterium; Models, Molecular; Mutagenesis, Site-Directed; Mutation; NAD; Nicotinamide-Nucleotide Adenylyltransferase; Phosphates; Protein Conformation | 2003 |
Occurrence of two different glutamate dehydrogenase activities in the halophilic bacterium Salinibacter ruber.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Bacterial Proteins; Bacteroidetes; Enzyme Activation; Enzyme Stability; Glutamate Dehydrogenase; Glutamic Acid; Histidine; Hydrogen-Ion Concentration; Ketoglutaric Acids; Leucine; NAD; NADP; Phenylalanine; Potassium Chloride; Sodium Chloride; Substrate Specificity | 2003 |
EFFECT OF INDOLES AND IMIDAZOLES, INCLUDING SEROTONIN AND HISTAMINE, ON THE MORPHOLOGY AND OXIDATIVE PHOSPHORYLATION OF GUINEA PIG LIVER MITOCHONDRIA.
Topics: Guinea Pigs; Histamine; Histidine; Imidazoles; Indoles; Liver; Metabolism; Mitochondria; Mitochondria, Liver; NAD; Oxidative Phosphorylation; Research; Serotonin | 1964 |
NONCOVALENT INTERACTIONS BETWEEN AMINO ACID SIDE CHAINS AND A COENZYME MODEL.
Topics: Amino Acids; Coenzymes; Fluorescence; Fluorometry; Histidine; Imidazoles; Indoles; Lysine; Methionine; NAD; Phenols; Phenylalanine; Pyridines; Research; Spectrum Analysis; Tyramine; Tyrosine | 1964 |
[ON THE DETERMINATION OF ACTIVE SITES OF CERTAIN ENZYMES. VI. A STUDY OF INHIBITION IN A REVERSIBLE REACTION].
Topics: Alcohol Oxidoreductases; Aspartate Aminotransferases; Catalytic Domain; Chemical Phenomena; Chemistry; Enzyme Inhibitors; Glutamate Dehydrogenase; Histidine; Imidazoles; Iron; Isocitrate Dehydrogenase; Kinetics; L-Lactate Dehydrogenase; NAD; Nitrogen; Pyruvates; Research; Sulfides; Zinc | 1964 |
EFFECT OF ALPHA-METHYLHISTIDINE ON THE CONTROL OF HISTIDINE SYNTHESIS.
Topics: Amino Acids; Enterobacter aerogenes; Escherichia coli; Histidine; Lyases; Metabolism; Methylhistidines; NAD; Ornithine; Ornithine Carbamoyltransferase; Oxidoreductases; Research; RNA; RNA, Bacterial; Transferases | 1964 |
CHARACTERISTICS OF BOUND PHOSPHOHISTIDINE LABELING IN MITOCHONDRIA.
Topics: Adenosine Triphosphate; Antimetabolites; Antimycin A; Dinitrophenols; Hexokinase; Histidine; Hydroxylamines; Liver; Metabolism; Mitochondria; NAD; Oligomycins; Phosphates; Phosphorus Isotopes; Rats; Research | 1965 |
Yeast life-span extension by calorie restriction is independent of NAD fluctuation.
Topics: Acetaldehyde; Aerobiosis; Bacterial Proteins; Caloric Restriction; CCAAT-Binding Factor; Culture Media; DNA-Binding Proteins; Genes, Fungal; Genes, Reporter; Histidine; Histone Deacetylases; Hydro-Lyases; Longevity; Magnetic Resonance Spectroscopy; NAD; Recombinant Fusion Proteins; Repressor Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Silent Information Regulator Proteins, Saccharomyces cerevisiae; Sirtuin 1; Sirtuin 2; Sirtuins; Transcription Factors | 2003 |
Chemical modification of catalytically essential functional groups of NAD-dependent hydrogenase from Ralstonia eutropha H16.
Topics: Cupriavidus necator; Cysteine; Diethyl Pyrocarbonate; Histidine; Hydrogen-Ion Concentration; Hydrogenase; Iodoacetamide; Kinetics; NAD | 2003 |
A novel NADH-linked l-xylulose reductase in the l-arabinose catabolic pathway of yeast.
Topics: Arabinose; Ascomycota; Blotting, Northern; Chromatography, High Pressure Liquid; DNA, Complementary; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Gene Library; Histidine; Kinetics; Molecular Sequence Data; NAD; Oxygen; Pentose Phosphate Pathway; Pentosephosphates; Protein Conformation; Saccharomyces cerevisiae; Substrate Specificity; Sugar Alcohol Dehydrogenases; Sugar Alcohols; Time Factors; Xylulose | 2004 |
Participation of histidine-51 in catalysis by horse liver alcohol dehydrogenase.
Topics: Alcohol Dehydrogenase; Amino Acid Substitution; Animals; Catalytic Domain; Crystallography, X-Ray; Deuterium Exchange Measurement; Glutamine; Histidine; Horses; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Liver; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; NAD | 2004 |
Structure of a cDNA for Ciona Cytochrome b(5) and the ubiquitous expression of mRNA in embryonic tissues.
Topics: Amino Acid Sequence; Animals; Base Sequence; Ciona intestinalis; Cloning, Molecular; Cytochromes b5; DNA, Complementary; Gene Expression; Heme; Histidine; Humans; Molecular Sequence Data; NAD; Nucleic Acid Conformation; Nucleic Acid Hybridization; Oxidoreductases; Recombinant Proteins; RNA, Messenger | 2004 |
A disorder to order transition accompanies catalysis in retinaldehyde dehydrogenase type II.
Topics: Aldehyde Oxidoreductases; Animals; Binding Sites; Catalysis; Crystallography, X-Ray; Escherichia coli; Histidine; Kinetics; Mice; Models, Molecular; Mutagenesis, Site-Directed; Mutation; NAD; Plasmids; Protein Conformation; Protein Structure, Secondary; Retinal Dehydrogenase; Spectrometry, Fluorescence; Spectrophotometry; Substrate Specificity; Time Factors; Transcription, Genetic; Tretinoin; X-Rays | 2004 |
The earliest events in protein folding: a structural requirement for ultrafast folding in cytochrome C.
Topics: Animals; Cytochromes c; Ferric Compounds; Guanidine; Histidine; Kinetics; Metalloproteins; Myocardium; NAD; Optical Rotation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Tuna | 2004 |
Aminobacter aminovorans NADH:flavin oxidoreductase His140: a highly conserved residue critical for NADH binding and utilization.
Topics: Alphaproteobacteria; Amino Acid Sequence; Anaerobiosis; Flavins; FMN Reductase; Histidine; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Oxidation-Reduction; Sequence Alignment; Spectrum Analysis | 2004 |
Histidine 129 in the 75-kDa subunit of mitochondrial complex I from Yarrowia lipolytica is not a ligand for [Fe4S4] cluster N5 but is required for catalytic activity.
Topics: Amino Acid Sequence; Catalysis; Electron Spin Resonance Spectroscopy; Electron Transport Complex I; Histidine; Hydrogenase; Iron-Sulfur Proteins; Ligands; Molecular Sequence Data; Molecular Weight; NAD; Protein Structure, Tertiary; Protein Subunits; Sequence Deletion; Yarrowia | 2005 |
Kinetic properties and metabolic contributions of yeast mitochondrial and cytosolic NADP+-specific isocitrate dehydrogenases.
Topics: Carbon; Carboxylic Acids; Catalysis; Cytosol; Electrophoresis; Genetic Complementation Test; Glucose; Glutamic Acid; Glycerol; Histidine; Hydrogen-Ion Concentration; Immunoblotting; Isocitrate Dehydrogenase; Isocitrates; Ketoglutaric Acids; Kinetics; Lactates; NAD; NADP; Phenotype; Plasmids; Protein Isoforms; Saccharomyces cerevisiae; Time Factors | 2005 |
Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc.
Topics: Amino Acid Sequence; Blotting, Western; Catalysis; Cloning, Molecular; Cysteine; D-Xylulose Reductase; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Ethanol; Fermentation; Histidine; Hot Temperature; Immunoblotting; Kinetics; Ligands; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; NAD; NADP; Pichia; Protein Structure, Tertiary; Recombinant Proteins; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Spectrophotometry; Substrate Specificity; Sugar Alcohol Dehydrogenases; Temperature; Time Factors; Xylose; Zinc | 2005 |
Identification of key amino acids responsible for the substantially higher affinities of human type 1 3beta-hydroxysteroid dehydrogenase/isomerase (3beta-HSD1) for substrates, coenzymes, and inhibitors relative to human 3beta-HSD2.
Topics: 3-Hydroxysteroid Dehydrogenases; Allosteric Site; Amino Acid Sequence; Androstenols; Animals; Arginine; Baculoviridae; Blotting, Western; Catalysis; Catalytic Domain; Cell Line; Dihydrotestosterone; DNA Primers; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Glutamine; Histidine; Humans; Insecta; Kinetics; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; NAD; Protein Binding; Protein Conformation; Sequence Homology, Amino Acid; Structure-Activity Relationship; Substrate Specificity; Tissue Distribution | 2005 |
The approach to the Michaelis complex in lactate dehydrogenase: the substrate binding pathway.
Topics: Ammonium Sulfate; Animals; Binding Sites; Catalysis; Entropy; Histidine; Hydrogen Bonding; Kinetics; L-Lactate Dehydrogenase; Lasers; Macromolecular Substances; Models, Chemical; Models, Statistical; Mutation; Myocardium; NAD; Organic Chemicals; Protein Binding; Protein Conformation; Signal Transduction; Spectrophotometry; Static Electricity; Substrate Specificity; Swine; Temperature; Thermodynamics; Time Factors | 2005 |
Structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum.
Topics: Amino Acid Sequence; Animals; Cloning, Molecular; Crystallography, X-Ray; Glyceraldehyde-3-Phosphate Dehydrogenases; Histidine; Models, Molecular; Molecular Sequence Data; Molecular Structure; NAD; Oligopeptides; Plasmodium falciparum; Protein Conformation; Recombinant Proteins; Sequence Alignment | 2005 |
Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase.
Topics: Benzene; Electron Transport; Flavin-Adenine Dinucleotide; Flavins; Gene Expression; Histidine; Hydrogen-Ion Concentration; Kinetics; NAD; Oxidation-Reduction; Oxidoreductases; Oxygen; Oxygenases; Pseudomonas putida; Styrene; Substrate Specificity | 2005 |
The Saccharomyces cerevisiae COQ10 gene encodes a START domain protein required for function of coenzyme Q in respiration.
Topics: Amino Acid Sequence; Chromatography, High Pressure Liquid; Coenzymes; Cytochrome Reductases; DNA Primers; DNA, Complementary; Electron Transport; Electron Transport Complex IV; Electrons; Gene Expression Regulation, Fungal; Genetic Complementation Test; Genotype; Histidine; Humans; Lipids; Mitochondria; Models, Genetic; Molecular Sequence Data; Multienzyme Complexes; Mutation; NAD; NADH, NADPH Oxidoreductases; Open Reading Frames; Oxygen; Oxygen Consumption; Phenotype; Plasmids; Protein Binding; Protein Biosynthesis; Protein Structure, Tertiary; Quinones; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Succinates; Ubiquinone | 2005 |
Sir2 protein deacetylases: evidence for chemical intermediates and functions of a conserved histidine.
Topics: Acetylation; Adenosine Diphosphate Ribose; Alanine; Binding Sites; Catalysis; Histidine; Hydrogen-Ion Concentration; Kinetics; Mutation; NAD; Protein Conformation; Sirtuins; Spectrometry, Mass, Electrospray Ionization; Substrate Specificity; Thermodynamics | 2006 |
Effect of co-existing biologically relevant molecules and ions on DNA photocleavage caused by pyrene and its derivatives.
Topics: DNA Damage; DNA, Superhelical; Electrophoresis, Agar Gel; Glutamic Acid; Histidine; Iodine; Ions; Metals; Mutagenicity Tests; NAD; Photochemistry; Pyrenes; Riboflavin; Ultraviolet Rays | 2005 |
Role of the His57-Glu214 ionic couple located in the active site of Mycobacterium tuberculosis FprA.
Topics: Amino Acid Sequence; Anaerobiosis; Binding Sites; Crystallography, X-Ray; Enzyme Stability; Flavin-Adenine Dinucleotide; Glutamic Acid; Histidine; Hot Temperature; Kinetics; Mycobacterium tuberculosis; NAD; NADH, NADPH Oxidoreductases; NADP; Oxidation-Reduction | 2006 |
Improving the purification of NAD+-dependent formate dehydrogenase from Candida methylica.
Topics: Biotechnology; Candida; Catalysis; Chromatography, Ion Exchange; Cloning, Molecular; Formate Dehydrogenases; Genes, Fungal; Genetic Vectors; Histidine; Kinetics; Mutagenesis, Site-Directed; NAD; Oxidation-Reduction; Recombinant Proteins; Spectrophotometry, Ultraviolet | 2007 |
One-step versus stepwise mechanism in protonated amino acid-promoted electron-transfer reduction of a quinone by electron donors and two-electron reduction by a dihydronicotinamide adenine dinucleotide analogue. Interplay between electron transfer and hyd
Topics: Amino Acids; Anions; Benzoquinones; Electron Spin Resonance Spectroscopy; Electron Transport; Electrons; Histidine; Hydrogen Bonding; Kinetics; Models, Chemical; NAD; Oxidation-Reduction; Protons; Quinones | 2008 |
Prebiotic origin of glycolytic metabolism: histidine and cysteine can produce acetyl CoA from glucose via reactions homologous to non-phosphorylated Entner-Doudoroff pathway.
Topics: Acetyl Coenzyme A; Amino Acids; Biochemistry; Catalysis; Chromatography, Thin Layer; Cysteine; Gluconates; Glucose; Glycolysis; Histidine; Mass Spectrometry; Models, Biological; NAD; Phosphorylation; Time Factors | 2008 |
A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis.
Topics: Adenosine Triphosphate; Catalysis; Cross-Linking Reagents; Cysteine; Electrochemistry; Escherichia coli; Histidine; Hydrolysis; Kinetics; Models, Biological; Molecular Conformation; Mutation; NAD; Plasmids; Proton-Translocating ATPases | 2008 |
Crystal structures of Mycobacterium tuberculosis S-adenosyl-L-homocysteine hydrolase in ternary complex with substrate and inhibitors.
Topics: Adenosine; Adenosylhomocysteinase; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Histidine; Homocysteine; Models, Molecular; Mycobacterium tuberculosis; NAD; Protein Structure, Tertiary | 2008 |
The crystal structure of Aquifex aeolicus prephenate dehydrogenase reveals the mode of tyrosine inhibition.
Topics: Bacteria; Catalysis; Catalytic Domain; Crystallography, X-Ray; Histidine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; NAD; Prephenate Dehydrogenase; Protein Conformation; Tyrosine | 2009 |
Cineole biodegradation: molecular cloning, expression and characterisation of (1R)-6beta-hydroxycineole dehydrogenase from Citrobacter braakii.
Topics: Biocatalysis; Citrobacter; Cloning, Molecular; Cyclohexanols; Eucalyptol; Histidine; Kinetics; Monoterpenes; NAD; Oligopeptides; Oxidoreductases; Protein Binding; Recombinant Proteins; Stereoisomerism; Substrate Specificity | 2010 |
Expression and purification of untagged and histidine-tagged folate-dependent tRNA:m5U54 methyltransferase from Bacillus subtilis.
Topics: Bacillus subtilis; Bacterial Proteins; Chromatography, Affinity; Chromatography, Gel; Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Histidine; Methylation; Models, Molecular; Molecular Weight; Mutation; NAD; Oxidation-Reduction; Recombinant Fusion Proteins; tRNA Methyltransferases | 2010 |
Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae.
Topics: Amino Acid Substitution; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Deuterium; Enzyme Stability; Histidine; Hydrogen-Ion Concentration; Kinetics; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins; NAD; Protein Conformation; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Saccharopine Dehydrogenases; Viscosity | 2012 |
The PduQ enzyme is an alcohol dehydrogenase used to recycle NAD+ internally within the Pdu microcompartment of Salmonella enterica.
Topics: Alcohol Dehydrogenase; Amino Acid Sequence; Gene Deletion; Histidine; Molecular Sequence Data; NAD; Oligopeptides; Propylene Glycol; Salmonella enterica; Transduction, Genetic | 2012 |
Exploration of CP12 conformational changes and of quaternary structural properties using electrospray ionization traveling wave ion mobility mass spectrometry.
Topics: Chlamydomonas; Chloroplast Proteins; Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); Histidine; NAD; Oxidation-Reduction; Protein Structure, Quaternary; Recombinant Fusion Proteins; Spectrometry, Mass, Electrospray Ionization | 2013 |
A biochemical correlate of dimorphism in a zygomycete Benjaminiella poitrasii: characterization of purified NAD-dependent glutamate dehydrogenase, a target for antifungal agents.
Topics: Ammonium Chloride; Antifungal Agents; Candida albicans; Catalysis; Chromatography, Agarose; Drug Evaluation, Preclinical; Fungal Proteins; Glutamate Dehydrogenase; Glutamic Acid; Histidine; Hyphae; Isoelectric Point; Ketoglutaric Acids; Lysine; Molecular Targeted Therapy; Molecular Weight; Mucorales; NAD; Phosphorylation; Protein Processing, Post-Translational; Substrate Specificity; Triazoles; Yarrowia | 2013 |
Spectrophotometric detection of histidine and lysine using combined enzymatic reactions.
Topics: Amino Acyl-tRNA Synthetases; Histidine; Histidine-tRNA Ligase; Hydrogen-Ion Concentration; Lysine; Lysine-tRNA Ligase; NAD; Spectrophotometry | 2013 |
Biochemical characterization of TyrA enzymes from Ignicoccus hospitalis and Haemophilus influenzae: A comparative study of the bifunctional and monofunctional dehydrogenase forms.
Topics: Amino Acid Sequence; Bacterial Proteins; Chorismate Mutase; Desulfurococcaceae; Escherichia coli; Haemophilus influenzae; Histidine; Multienzyme Complexes; NAD; NADP; Prephenate Dehydrogenase; Tyrosine | 2017 |
Structure of Urocanate Hydratase from the protozoan Trypanosoma cruzi.
Topics: Amino Acid Sequence; Bacillus subtilis; Cloning, Molecular; Crystallization; Geobacillus; Histidine; NAD; Protein Conformation, alpha-Helical; Pseudomonas putida; Reproducibility of Results; Sequence Alignment; Trypanosoma cruzi; Urocanate Hydratase | 2020 |
The SensorOverlord predicts the accuracy of measurements with ratiometric biosensors.
Topics: Animals; Biochemistry; Biosensing Techniques; Fluorescence; Glutathione; Histidine; Hydrogen-Ion Concentration; Microscopy, Fluorescence; NAD; NADP; Oxidation-Reduction; Predictive Value of Tests | 2020 |
Experimental Clarification of PRPS-1 Structural Essentials.
Topics: Diphosphates; Histidine; Molecular Docking Simulation; NAD; NADP; Nucleotides; Phosphates; Phosphoribosyl Pyrophosphate; Purines; Pyridines; Pyrimidines; Ribose-Phosphate Pyrophosphokinase; Tryptophan | 2022 |
Structural Insights into
Topics: Adenosine Diphosphate Ribose; Histidine; Molecular Dynamics Simulation; NAD; Peptide Elongation Factor 2; Pseudomonas aeruginosa; Pseudomonas aeruginosa Exotoxin A | 2023 |