nad has been researched along with 3-acetylpyridine adenine dinucleotide in 67 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 21 (31.34) | 18.7374 |
| 1990's | 34 (50.75) | 18.2507 |
| 2000's | 10 (14.93) | 29.6817 |
| 2010's | 2 (2.99) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Benziman, M; Kornfeld, S; Milner, Y | 1 |
| Jackson, JB; Palmer, T | 1 |
| Engel, PC; Parker, DM; Syed, SE | 1 |
| Burgner, J; Callender, R; Deng, H | 1 |
| Cleland, WW; Cook, PF; Gavva, SR; Harris, BG; Urbauer, JL; Weiss, PM | 1 |
| Grimshaw, CE; Putney, CG; Shahbaz, M | 1 |
| Ferrier, B | 1 |
| Coburn, J; Gill, DM | 1 |
| Gill, DM; Tamir, A | 1 |
| Morrison, JF; Stone, SR | 1 |
| Heine, HG; Richarme, G | 1 |
| Bragg, PD; Clarke, DM | 1 |
| Hatefi, Y; Phelps, DC | 1 |
| Engel, PC; Hornby, DP | 1 |
| Aitchison, MJ; Engel, PC; Hornby, DP | 1 |
| Ingledew, WJ; Ohnishi, T | 1 |
| Kamlay, MT; Shore, JD | 1 |
| Garel, JR; Müller, K | 1 |
| Cleland, WW; Hermes, JD; Morrical, SW; O'Leary, MH | 1 |
| Fisher, RR; Pennington, RM | 1 |
| Fioravanti, CF; McKelvey, JR | 1 |
| Chen, S; Guillory, RJ; Jeng, SJ | 1 |
| Boland, MJ | 1 |
| Earle, SR; Fisher, RR; Wu, LN | 1 |
| Henis, YI; Levitzki, A | 1 |
| Claiborne, A; Crane, EJ; Parsonage, D; Poole, LB | 1 |
| Bragg, PD; Glavas, NA | 1 |
| Hatefi, Y; Yamaguchi, M | 2 |
| Bizouarn, T; Cotton, NP; Grimley, RL; Hutton, M; Jackson, JB; Stilwell, SN | 1 |
| Hu, X; Persson, A; Rydström, J; Zhang, JW | 1 |
| Bizouarn, T; Day, JM; Hutton, M; Jackson, JB | 1 |
| Fristedt, U; Persson, B; Rydström, J | 1 |
| Cook, PF; Karsten, WE | 1 |
| Bizouarn, T; Jackson, JB | 1 |
| Bhatnagar, A; Liu, SQ; Srivastava, SK | 1 |
| Cotton, NP; Jackson, JB; Palmer, T; Thomas, CM; Williams, R | 1 |
| Kasper, CB; Shen, AL | 1 |
| Bizouarn, T; Diggle, C; Jackson, JB | 1 |
| Cavaleyra, M; Monteny, N; Peltre, G; Riandey, MF; Sannier, C | 1 |
| Gleitz, J; Peters, T; Tosch, C | 1 |
| Bizouarn, T; Cotton, NP; Diggle, C; Jackson, JB | 1 |
| Bragg, PD | 1 |
| Dafforn, TR; Hewitt, CO; Holbrook, JJ; Sessions, RB | 1 |
| Bizouarn, T; Jackson, JB; Stilwell, SN | 1 |
| Clarke, AR; Dewar, V; Holbrook, JJ; Sessions, RB | 1 |
| Bizouarn, T; Diggle, C; Grimley, R; Jackson, JB; Thomas, CM | 1 |
| Bizouarn, T; Cotton, NP; Jackson, JB; Stilwell, S; Venning, J | 1 |
| Bragg, PD; Hou, C | 2 |
| Bradshaw, DE; Cleland, WW; Urbauer, JL | 1 |
| Vinogradov, AD; Zakharova, NV; Zharova, TV | 1 |
| Claiborne, A; Mallett, TC; Parsonage, D | 1 |
| Axelsson, M; Bizouarn, T; Egorov, MV; Fjellström, O; Ivanova, MV; Korneenko, TV; Pestov, NB; Rydström, J; Shakhparonov, M | 1 |
| Kissner, R; Koppenol, WH; Prütz, WA; Rüegger, H | 1 |
| Zakharova, NV | 1 |
| Imai, T | 1 |
| BRUNNEMANN, A; COPER, H; HERKEN, H | 1 |
| BRUNNEMANN, A; COPER, H | 1 |
| Elling, RA; Kavanagh, KL; Wilson, DK | 1 |
| Brady, RL; Chaikuad, A; Conners, R; Fairweather, V; Joseph-Horne, T; Turgut-Balik, D | 1 |
| Hirst, J; Yakovlev, G | 1 |
| Bhagwat, AS; Roy, TW | 1 |
| Hedstrom, L; Josephine, HR; Riera, TV; Wang, W | 1 |
| Birrell, JA; Hirst, J; Yakovlev, G | 1 |
| Lee, HJ; Lee, SH; Park, CB; Won, K | 1 |
| Birrell, JA; Hirst, J | 1 |
67 other study(ies) available for nad and 3-acetylpyridine adenine dinucleotide
| Article | Year |
|---|---|
Alpha-ketoglutarate dehydrogenase complex of Acetobacter xylinum. Purification and regulatory properties.
Topics: Adenosine Monophosphate; Allosteric Regulation; Binding, Competitive; Coenzyme A; Gluconacetobacter xylinus; Hydrogen-Ion Concentration; Ketoglutarate Dehydrogenase Complex; Ketone Oxidoreductases; Kinetics; Magnesium; Molecular Weight; NAD; Thiamine Pyrophosphate | 1977 |
Nicotinamide nucleotide transhydrogenase from Rhodobacter capsulatus; the H+/H- ratio and the activation state of the enzyme during reduction of acetyl pyridine adenine dinucleotide.
Topics: Membrane Potentials; NAD; NADP Transhydrogenases; Oxidation-Reduction; Protein Conformation; Rhodobacter capsulatus | 1992 |
Functional studies of a glutamate dehydrogenase with known three-dimensional structure: steady-state kinetics of the forward and reverse reactions catalysed by the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum.
Topics: Amines; Catalysis; Clostridium; Glutamate Dehydrogenase; Kinetics; NAD; Protein Conformation; Substrate Specificity | 1991 |
Raman spectroscopic studies of NAD coenzymes bound to malate dehydrogenases by difference techniques.
Topics: Coenzymes; Cytoplasm; L-Lactate Dehydrogenase; Malate Dehydrogenase; Mitochondria; NAD; Protein Binding; Spectrum Analysis, Raman | 1991 |
Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction.
Topics: Animals; Ascaris; Carbon Isotopes; Chickens; Decarboxylation; Deuterium; Kinetics; Liver; Malate Dehydrogenase; Malates; NAD; NADP; Oxidation-Reduction; Substrate Specificity | 1991 |
Spectroscopic and kinetic characterization of nonenzymic and aldose reductase mediated covalent NADP-glycolaldehyde adduct formation.
Topics: Acetaldehyde; Aldehyde Reductase; Animals; Cattle; Kinetics; NAD; Oxidation-Reduction; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet | 1990 |
An enzymatic cycling method for 3-acetylpyridine adenine dinucleotide to increase the sensitivity of enzymatic methods which employ this NAD analog.
Topics: Coenzymes; Fluorometry; Indicators and Reagents; L-Lactate Dehydrogenase; Malate Dehydrogenase; Malates; NAD; Oxidation-Reduction | 1990 |
ADP-ribosylation of membrane proteins by bacterial toxins in the presence of NAD glycohydrolase.
Topics: Adenosine Diphosphate Ribose; Animals; Brain Chemistry; Cattle; Cholera Toxin; Columbidae; Drug Synergism; Erythrocyte Membrane; GTP-Binding Proteins; Isoniazid; Membrane Proteins; Mice; NAD; NAD+ Nucleosidase; Pertussis Toxin; Swine; Virulence Factors, Bordetella | 1988 |
ADP-ribosylation by cholera toxin of membranes derived from brain modifies the interaction of adenylate cyclase with guanine nucleotides and NaF.
Topics: Adenosine Diphosphate Ribose; Adenylyl Cyclases; Animals; Brain; Cattle; Caudate Nucleus; Cell Membrane; Cholera Toxin; Coenzymes; Enzyme Activation; GTP-Binding Proteins; Guanine Nucleotides; Guanosine Triphosphate; Guanylyl Imidodiphosphate; Isoniazid; Kinetics; NAD; NAD+ Nucleosidase; Sodium Fluoride | 1988 |
Dihydrofolate reductase from Escherichia coli: the kinetic mechanism with NADPH and reduced acetylpyridine adenine dinucleotide phosphate as substrates.
Topics: Deuterium; Escherichia coli; Folic Acid; Hydrogen-Ion Concentration; Kinetics; NAD; NADP; Tetrahydrofolate Dehydrogenase; Viscosity | 1988 |
Galactose- and maltose-stimulated lipoamide dehydrogenase activities related to the binding-protein-dependent transport of galactose and maltose in toluenized cells of Escherichia coli.
Topics: ATP-Binding Cassette Transporters; Biological Transport; Calcium-Binding Proteins; Carrier Proteins; Dihydrolipoamide Dehydrogenase; Edetic Acid; Enzyme Activation; Escherichia coli; Escherichia coli Proteins; Galactose; Genes, Bacterial; Maltose; Maltose-Binding Proteins; Monosaccharide Transport Proteins; Mutation; NAD; Operon; Periplasmic Binding Proteins; Thioctic Acid; Toluene | 1986 |
Purification and properties of reconstitutively active nicotinamide nucleotide transhydrogenase of Escherichia coli.
Topics: Allosteric Site; Catalysis; Cytoplasm; Dicyclohexylcarbodiimide; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; NAD; NADH, NADPH Oxidoreductases; NADP; NADP Transhydrogenases; Oxidation-Reduction; Peptide Fragments; Solubility; Spectrometry, Fluorescence | 1985 |
Effects of N,N'-dicyclohexylcarbodiimide and N-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline on hydride ion transfer and proton translocation activities of mitochondrial nicotinamidenucleotide transhydrogenase.
Topics: Animals; Binding Sites; Carbodiimides; Dicyclohexylcarbodiimide; In Vitro Techniques; Mitochondria; NAD; NADH, NADPH Oxidoreductases; NADP; NADP Transhydrogenases; Protons; Quinolines | 1984 |
A kinetic study of the oxidative deamination of L-glutamate by Peptostreptococcus asaccharolyticus glutamate dehydrogenase using a variety of coenzymes.
Topics: Coenzymes; Deamination; Glutamate Dehydrogenase; Glutamates; Glutamic Acid; Hydrogen-Ion Concentration; Kinetics; NAD; Oxidation-Reduction; Peptostreptococcus | 1984 |
The kinetic mechanism of ox liver glutamate dehydrogenase in the presence of the allosteric effector ADP. The oxidative deamination of L-glutamate.
Topics: Adenosine Diphosphate; Animals; Cattle; Deamination; Glutamate Dehydrogenase; Glutamates; Glutamic Acid; Kinetics; Liver; NAD; Oxidation-Reduction | 1984 |
An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria.
Topics: Adenosine Triphosphate; Animals; Electron Spin Resonance Spectroscopy; Electron Transport; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Membrane Potentials; Metalloproteins; Mitochondria, Heart; NAD; Oxidation-Reduction; Potentiometry; Thermodynamics | 1980 |
Transient kinetic studies of substrate inhibition in the horse liver alcohol dehydrogenase reaction.
Topics: Alcohol Dehydrogenase; Alcohol Oxidoreductases; Animals; Binding Sites; Ethanol; Horses; Kinetics; Liver; NAD; Oxidation-Reduction; Substrate Specificity | 1983 |
The interaction between Escherichia coli aspartokinase-homoserine dehydrogenase and 3-acetylpyridine-adenine dinucleotide phosphate (reduced), an analog of NADPH.
Topics: Aspartokinase Homoserine Dehydrogenase; Binding Sites; Escherichia coli; Kinetics; Multienzyme Complexes; NAD; NADP; Oxidation-Reduction; Protein Binding | 1984 |
Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 2. Formate dehydrogenase.
Topics: Aldehyde Oxidoreductases; Carbon Isotopes; Chemical Phenomena; Chemistry; Deuterium; Formate Dehydrogenases; Formates; Kinetics; NAD; Nitrogen Isotopes; Oxidation-Reduction; Oxygen Isotopes; Saccharomyces cerevisiae | 1984 |
Reconstituted mitochondrial transhydrogenase is a transmembrane protein.
Topics: Animals; Cattle; Liposomes; Mitochondria, Heart; NAD; NADH, NADPH Oxidoreductases; NADP; NADP Transhydrogenases; Photic Stimulation; Taurine | 1983 |
Coupling of "malic" enzyme and NADPH:NAD transhydrogenase in the energetics of Hymenolepis diminuta (Cestoda).
Topics: Animals; Coenzymes; Electron Transport; Energy Metabolism; Hymenolepis; Malate Dehydrogenase; Male; Mitochondria; NAD; NADH, NADPH Oxidoreductases; NADP Transhydrogenases; Oxidation-Reduction; Rats; Rats, Inbred Strains | 1984 |
Current applications of the photoaffinity technique to the study of the structure of complex I.
Topics: Affinity Labels; Alcohol Oxidoreductases; Animals; Azides; beta-Alanine; Cattle; Magnetic Resonance Spectroscopy; NAD; NAD(P)H Dehydrogenase (Quinone); NADH, NADPH Oxidoreductases; NADP; Photochemistry; Pyrimidine Nucleotides; Quinone Reductases; Ubiquinone | 1980 |
NADH-dependent glutamate synthase from lupin nodules. Reactions with oxidised and reduced 3-acetylpyridine-adenine dinucleotide.
Topics: Coenzymes; Glutamate Synthase; Kinetics; NAD; Oxidation-Reduction; Plants; Spectrophotometry, Ultraviolet; Transaminases | 1981 |
Bovine heart mitochondrial transhydrogenase catalyzes an exchange reaction between NADH and NAD+.
Topics: Animals; Cattle; Coenzymes; Hydrogen-Ion Concentration; Kinetics; Mitochondria, Heart; NAD; NADH, NADPH Oxidoreductases; NADP Transhydrogenases; Oxidation-Reduction; Tritium | 1981 |
The sequential nature of the negative cooperativity in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase.
Topics: Adenosine Diphosphate Ribose; Adenosine Triphosphate; Animals; Binding, Competitive; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Macromolecular Substances; Muscles; NAD; Rabbits; Spectrometry, Fluorescence | 1980 |
Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms.
Topics: Catalysis; Coenzymes; Deuterium; Electrons; Enterococcus; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; NAD; Oxidation-Reduction; Peroxidases | 1995 |
The mechanism of hydride transfer between NADH and 3-acetylpyridine adenine dinucleotide by the pyridine nucleotide transhydrogenase of Escherichia coli.
Topics: Amino Acid Sequence; Escherichia coli; Hydrogen; Hydrogen-Ion Concentration; Molecular Sequence Data; NAD; NADP; NADP Transhydrogenases; Trypsin | 1995 |
Proton-translocating nicotinamide nucleotide transhydrogenase of Escherichia coli. Involvement of aspartate 213 in the membrane-intercalating domain of the beta subunit in energy transduction.
Topics: Amino Acid Sequence; Escherichia coli; Molecular Sequence Data; Mutation; NAD; NADP; NADP Transhydrogenases; Structure-Activity Relationship | 1995 |
The involvement of NADP(H) binding and release in energy transduction by proton-translocating nicotinamide nucleotide transhydrogenase from Escherichia coli.
Topics: Escherichia coli; Kinetics; NAD; NADP; NADP Transhydrogenases | 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 |
Kinetic resolution of the reaction catalysed by proton-translocating transhydrogenase from Escherichia coli as revealed by experiments with analogues of the nucleotide substrates.
Topics: Binding Sites; Dicyclohexylcarbodiimide; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protons; Solubility | 1994 |
Evidence for a nicotinamide nucleotide transhydrogenase in Klebsiella pneumoniae.
Topics: Animals; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Cattle; Cell Membrane; Coenzymes; Kinetics; Klebsiella pneumoniae; Mitochondria, Heart; NAD; NADP Transhydrogenases; Oxidation-Reduction; Submitochondrial Particles | 1994 |
Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation.
Topics: Animals; Ascaris; Carboxylic Acids; Catalysis; Chickens; Horses; Isotopes; Malate Dehydrogenase; NAD; NADP; Oxaloacetates; Oxidation-Reduction | 1994 |
The ratio of protons translocated/hydride ion equivalent transferred by nicotinamide nucleotide transhydrogenase in chromatophores from Rhodospirillum rubrum.
Topics: Bacterial Chromatophores; Coenzymes; Hydrogen-Ion Concentration; Kinetics; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protons; Rhodospirillum rubrum; Spectrophotometry, Ultraviolet | 1993 |
Bovine lens aldose reductase. pH-dependence of steady-state kinetic parameters and nucleotide binding.
Topics: Aldehyde Reductase; Animals; Cattle; Coenzymes; Hydrogen-Ion Concentration; Kinetics; Lens, Crystalline; Mathematics; Models, Theoretical; NAD; NADP; Oxidation-Reduction; Protein Binding; Substrate Specificity | 1993 |
Inhibition of proton-translocating transhydrogenase from photosynthetic bacteria by N,N'-dicyclohexylcarbodiimide.
Topics: Amino Acid Sequence; Binding Sites; Dicyclohexylcarbodiimide; Molecular Sequence Data; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Peptide Fragments; Rhodobacter capsulatus; Rhodospirillum rubrum | 1993 |
Role of Ser457 of NADPH-cytochrome P450 oxidoreductase in catalysis and control of FAD oxidation-reduction potential.
Topics: Base Sequence; Cytochrome c Group; Dithionite; DNA Primers; Electron Transport; Ferricyanides; Flavin-Adenine Dinucleotide; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; NADH, NADPH Oxidoreductases; NADP; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Polymerase Chain Reaction; Serine; Spectrophotometry | 1996 |
The binding of nucleotides to domain I proteins of the proton-translocating transhydrogenases from Rhodospirillum rubrum and Escherichia coli as measured by equilibrium dialysis.
Topics: Binding Sites; Coenzymes; Dialysis; Escherichia coli; NAD; NADP Transhydrogenases; Nucleotides; Peptide Fragments; Recombinant Proteins; Rhodospirillum rubrum | 1996 |
Lactate dehydrogenase as a marker of Plasmodium infection in malaria vector Anopheles.
Topics: Animals; Anopheles; Biomarkers; Female; Insect Vectors; Isoelectric Point; Isoenzymes; L-Lactate Dehydrogenase; Malaria; Mice; NAD; Plasmodium yoelii | 1996 |
Continuous enzyme-linked fluorometric detection of L-(+)-lactate released from rat brain vesicles under anoxic conditions.
Topics: Animals; Brain Chemistry; Calcium; Enzyme-Linked Immunosorbent Assay; Fura-2; Hypoxia, Brain; In Vitro Techniques; L-Lactate Dehydrogenase; Lactic Acid; Male; NAD; Oxygen Consumption; Rats; Rats, Wistar; Sodium; Spectrometry, Fluorescence; Tetrodotoxin | 1996 |
Properties of the purified, recombinant, NADP(H)-binding domain III of the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum.
Topics: Binding Sites; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Kinetics; Models, Chemical; NAD; NADP; NADP Transhydrogenases; Nucleotides; Protein Binding; Recombinant Proteins; Rhodospirillum rubrum; Spectrometry, Fluorescence; Spectrophotometry | 1996 |
Mechanism of hydride transfer during the reduction of 3-acetylpyridine adenine dinucleotide by NADH catalyzed by the pyridine nucleotide transhydrogenase of Escherichia coli.
Topics: Binding Sites; Escherichia coli; Kinetics; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protons | 1996 |
High cyclic transhydrogenase activity catalyzed by expressed and reconstituted nucleotide-binding domains of Rhodospirillum rubrum transhydrogenase.
Topics: Animals; Base Sequence; Binding Sites; Cattle; DNA Primers; Escherichia coli; In Vitro Techniques; Kinetics; Molecular Structure; Molecular Weight; NAD; NADP; NADP Transhydrogenases; Protein Conformation; Recombinant Proteins; Rhodospirillum rubrum | 1997 |
Protein engineering tests of a homology model of Plasmodium falciparum lactate dehydrogenase.
Topics: Amino Acid Sequence; Animals; Binding Sites; Drug Design; Geobacillus stearothermophilus; Kinetics; L-Lactate Dehydrogenase; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Plasmodium falciparum; Protein Engineering; Sequence Homology, Amino Acid; Structure-Activity Relationship | 1997 |
The reduction of acetylpyridine adenine dinucleotide by NADH: is it a significant reaction of proton-translocating transhydrogenase, or an artefact?
Topics: Binding Sites; Chromatophores; Escherichia coli; NAD; NADH, NADPH Oxidoreductases; Oxidation-Reduction | 1997 |
A model of Plasmodium falciparum lactate dehydrogenase and its implications for the design of improved antimalarials and the enhanced detection of parasitaemia.
Topics: Amino Acid Sequence; Animals; Antimalarials; Binding Sites; Crystallography, X-Ray; Drug Design; Geobacillus stearothermophilus; Gossypol; Humans; Kinetics; L-Lactate Dehydrogenase; Lactic Acid; Models, Chemical; Models, Molecular; Molecular Sequence Data; NAD; Plasmodium falciparum; Protein Structure, Tertiary; Sequence Alignment; Sequence Deletion; Stereoisomerism; Swine | 1997 |
Mutations at tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer.
Topics: Hydrogen; Mutation; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protein Binding; Recombinant Proteins; Rhodospirillum rubrum; Tyrosine | 1997 |
The pH dependences of reactions catalyzed by the complete proton-translocating transhydrogenase from Rhodospirillum rubrum, and by the complex formed from its recombinant nucleotide-binding domains.
Topics: Bacterial Chromatophores; Binding Sites; Electron Transport; Hydrogen-Ion Concentration; Kinetics; NAD; NADP; NADP Transhydrogenases; Protons; Recombinant Proteins; Rhodospirillum rubrum | 1997 |
Effect of truncation and mutation of the carboxyl-terminal region of the beta subunit on membrane assembly and activity of the pyridine nucleotide transhydrogenase of Escherichia coli.
Topics: Amino Acid Sequence; Cell Membrane; Escherichia coli; Kinetics; Molecular Sequence Data; Mutation; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protein Conformation; Sequence Deletion | 1998 |
Determination of the kinetic and chemical mechanism of malic enzyme using (2R,3R)-erythro-fluoromalate as a slow alternate substrate.
Topics: Animals; Carbon Isotopes; Catalysis; Cattle; Chickens; Coenzymes; Decarboxylation; Deuterium; Kinetics; Malate Dehydrogenase; Malates; NAD; NADP; Oxaloacetates; Rabbits; Substrate Specificity; Swine | 1998 |
Mutation of conserved polar residues in the transmembrane domain of the proton-pumping pyridine nucleotide transhydrogenase of Escherichia coli.
Topics: Amino Acid Sequence; Amino Acid Substitution; Asparagine; Bacterial Proteins; Coenzymes; Conserved Sequence; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Hydrogenation; Intracellular Membranes; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; NADP Transhydrogenases; Protein Structure, Tertiary; Proton Pumps | 1999 |
Kinetics of transhydrogenase reaction catalyzed by the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) imply more than one catalytic nucleotide-binding sites.
Topics: Animals; Binding Sites; Cattle; Electron Transport Complex I; Flavoproteins; Kinetics; Mitochondria, Heart; NAD; NADH, NADPH Oxidoreductases; NADP Transhydrogenases; Submitochondrial Particles | 1999 |
Equilibrium analyses of the active-site asymmetry in enterococcal NADH oxidase: role of the cysteine-sulfenic acid redox center.
Topics: Bacterial Proteins; Binding Sites; Coenzymes; Cysteine; Dithionite; Electron Transport; Enzyme Stability; Hydrogen-Ion Concentration; Multienzyme Complexes; Mutagenesis, Site-Directed; NAD; NADH, NADPH Oxidoreductases; NADP; Oxidation-Reduction; Recombinant Proteins; Serine; Spectrometry, Fluorescence; Sulfenic Acids | 1999 |
Interactions between the soluble domain I of nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum and transhydrogenase from Escherichia coli. Effects on catalytic and H+-pumping activities.
Topics: Amino Acid Sequence; Animals; Antibodies, Bacterial; Antibodies, Monoclonal; Bacterial Proteins; Catalysis; Detergents; Escherichia coli; Hydrogen-Ion Concentration; Liposomes; Mice; Mice, Inbred BALB C; Models, Molecular; Molecular Sequence Data; NAD; NADP; NADP Transhydrogenases; Protein Binding; Protein Conformation; Protein Denaturation; Protein Multimerization; Protein Structure, Tertiary; Protons; Recombinant Fusion Proteins; Rhodospirillum rubrum; Trypsin | 2000 |
On the irreversible destruction of reduced nicotinamide nucleotides by hypohalous acids.
Topics: Bromates; Chlorates; Hydrogen-Ion Concentration; Iodine Compounds; Kinetics; Magnetic Resonance Spectroscopy; Models, Chemical; NAD; Niacinamide; Nicotinamide Mononucleotide; Oxidation-Reduction; Oxygen; Pyridines; Time Factors | 2000 |
Kinetics of the transhydrogenase reaction catalyzed by mitochondrial NADH:ubiquinone oxidoreductase (complex I).
Topics: Adenosine Diphosphate Ribose; Anthraquinones; Catalysis; Electron Transport Complex I; Kinetics; Mitochondria; NAD; NADH, NADPH Oxidoreductases | 2002 |
Substrate specificity of mammalian pyridine nucleotide transglycosidases.
Topics: Animals; Cattle; Glycoside Hydrolases; Guinea Pigs; Hydrolysis; Kinetics; Liver; Multienzyme Complexes; N-Glycosyl Hydrolases; NAD; NADP; Niacin; Nicotinamide Mononucleotide; Rabbits; Spectrophotometry; Spleen; Substrate Specificity; Swine; Transferases | 2002 |
[Isolation of 3-acetylpyridine-adeninedinucleotide (3-APAD) from the brain of 3-acetylpyridine-poisoned rats].
Topics: Adenine Nucleotides; Animals; Brain; NAD; Niacin; Nicotinic Acids; Pyridines; Rats | 1962 |
[HYDROLYSIS OF NAD(P) AND BIOSYNTHESIS OF 3-APAD(P) BY BRAIN MICROSOMES OF DIFFERENT ANIMAL SPECIES].
Topics: Animals; Brain; Hydrolysis; Microsomes; NAD; NADP; Nucleotides; Research | 1965 |
Structure of Toxoplasma gondii LDH1: active-site differences from human lactate dehydrogenases and the structural basis for efficient APAD+ use.
Topics: Animals; Apoenzymes; Binding Sites; Catalysis; Coenzymes; Crystallography, X-Ray; Enzyme Inhibitors; Humans; Isoenzymes; L-Lactate Dehydrogenase; Lactic Acid; Muscle, Skeletal; Myocardium; NAD; Oxalic Acid; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Pyruvic Acid; Substrate Specificity; Toxoplasma | 2004 |
Structure of lactate dehydrogenase from Plasmodium vivax: complexes with NADH and APADH.
Topics: Animals; Binding Sites; Crystallography, X-Ray; Humans; Isoenzymes; L-Lactate Dehydrogenase; Models, Molecular; NAD; Plasmodium vivax; Protein Conformation | 2005 |
Transhydrogenation reactions catalyzed by mitochondrial NADH-ubiquinone oxidoreductase (Complex I).
Topics: Animals; Cattle; Electron Transport Complex I; Hydrogen; Mitochondria, Heart; NAD; NADP | 2007 |
Kinetic studies of Escherichia coli AlkB using a new fluorescence-based assay for DNA demethylation.
Topics: DNA; DNA Repair Enzymes; Escherichia coli Proteins; Formaldehyde; Kinetics; Mixed Function Oxygenases; NAD; Spectrometry, Fluorescence; Substrate Specificity | 2007 |
A kinetic alignment of orthologous inosine-5'-monophosphate dehydrogenases.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cryptosporidium parvum; Guanosine Monophosphate; IMP Dehydrogenase; Inosine Monophosphate; Kinetics; Models, Molecular; Molecular Conformation; Molecular Sequence Data; NAD; Protein Binding; Ribonucleotides; Xanthine | 2008 |
Reactions of the flavin mononucleotide in complex I: a combined mechanism describes NADH oxidation coupled to the reduction of APAD+, ferricyanide, or molecular oxygen.
Topics: Animals; Binding, Competitive; Catalysis; Cattle; Electron Transport Complex I; Ferricyanides; Flavin Mononucleotide; Kinetics; NAD; Oxidation-Reduction; Oxygen; Protein Binding; Ruthenium Compounds | 2009 |
Artificial electron carriers for photoenzymatic synthesis under visible light.
Topics: Coenzymes; Electrons; Light; NAD; Oxidation-Reduction | 2012 |
Investigation of NADH binding, hydride transfer, and NAD(+) dissociation during NADH oxidation by mitochondrial complex I using modified nicotinamide nucleotides.
Topics: Adenosine; Adenosine Diphosphate; Adenosine Diphosphate Ribose; Adenosine Monophosphate; Animals; Binding, Competitive; Cattle; Coenzymes; Electron Transport Complex I; Flavins; Hydrogen; Kinetics; Mitochondria, Heart; Models, Molecular; NAD; Nicotinamide Mononucleotide; Oxidation-Reduction; Protein Binding | 2013 |