phenylalanine has been researched along with nadp in 49 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 23 (46.94) | 18.7374 |
| 1990's | 10 (20.41) | 18.2507 |
| 2000's | 13 (26.53) | 29.6817 |
| 2010's | 3 (6.12) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Shibata, Y | 1 |
| Appleman, JR; Beard, WA; Blakley, RL; Delcamp, TJ; Freisheim, JH; Huang, SM | 1 |
| Dunn, SM; Howell, EE; Lanigan, TM | 1 |
| Appleman, JR; Blakley, RL; Delcamp, TJ; Freisheim, JH; Prendergast, NJ | 1 |
| Birdsall, B; Feeney, J; Hammond, SJ; Roberts, GC; Searle, MS | 1 |
| Benkovic, SJ; Chen, JT; Taira, K; Tu, CP | 1 |
| Akino, M; Hasegawa, H; Nakanishi, N; Yamada, S | 1 |
| Huang, CY; Kaufman, S | 1 |
| Fisher, DB; Kaufman, S | 1 |
| Gamper, H; Moses, V | 1 |
| Benoiton, NL; D'lorio, A; Sharma, S; Tong, JH | 1 |
| Bondy, PK; Burrow, GN; Mulrow, PJ | 1 |
| Haljasmaa, O; Ross, SB | 1 |
| Ziegler, H; Ziegler, I | 1 |
| Kaufman, S | 3 |
| Gottlieb, D; Inoue, Y | 1 |
| Hecker, E; Marks, F | 1 |
| Kato, R | 1 |
| Benoiton, NL; D'Iorio, A; Tong, JH | 1 |
| Friedrich, B; Schlegel, HG | 1 |
| Keller, B; Keller, E; Lingens, F; Salcher, O | 1 |
| Appleman, JR; Blakley, RL; Nakano, T; Spencer, HT | 1 |
| Appleman, JR; Blakley, RL; Chunduru, SK; Cody, V; Luft, JR; Pangborn, W | 1 |
| Porter, TD | 1 |
| Bradrick, TD; Dion, A; Georghiou, S; Howell, EE; Linn, CE | 1 |
| Gekko, K; Hayashi, H; Kagamiyama, H; Ohmae, E; Tamura, Y; Ueno, H | 1 |
| Capdevila, JH; Falck, JR; Graham-Lorence, S; Helvig, C; Peterson, JA; Truan, G; Wei, S | 1 |
| Broger, C; D'Arcy, A; Dale, GE; DeHoogt, R; Hartman, PG; Jolidon, S; Kompis, I; Labhardt, AM; Langen, H; Locher, H; Oefner, C; Page, MG; Stüber, D; Then, RL; Wipf, B | 1 |
| Bunthol, C; Eppink, MH; Schreuder, HA; van Berkel, WJ | 1 |
| Bradrick, TD; Howell, EE; Seo, HS; West, FW | 1 |
| Daff, S; Sagami, I; Sato, Y; Shimizu, T | 1 |
| Blanchard, JS; Brunhuber, NM; Thoden, JB; Vanhooke, JL | 1 |
| Li, QS; Ogawa, J; Shimizu, S | 1 |
| Colman, RF; Huang, YC | 1 |
| Aykin-Burns, N; Ercal, N; Gurer-Orhan, H; McDonald, JD | 1 |
| Anderson, S; Banta, S; Jarnagin, A; Swanson, BA; Wu, S | 1 |
| Boitano, AE; Jones, JP; Rock, DA; Wahlstrom, JL | 1 |
| Arnold, P; Baker, ME; Frey, FJ; Odermatt, A; Tam, S; Yan, L | 1 |
| Bonete, MJ; Díaz, S; Ferrer, J; Oren, A; Pérez-Pomares, F | 1 |
| BRESNICK, E; YANG, HY | 1 |
| GAMBORG, OL; SIMPSON, FJ | 1 |
| Labrie, F; Lin, SX; Qiu, W; Zhou, M | 1 |
| Bergamini, CM; Cervellati, C; Cook, PF; Dallocchio, F | 1 |
| Petty, HR; Romero, R; Zhu, A | 1 |
| Debnar-Daumler, C; Heider, J; Schmitt, G; Seubert, A | 1 |
| Chhabra, A; Deshmukh, MV; Gokhale, RS; Haque, AS; Patel, KD; Sankaranarayanan, R | 1 |
| Binz, PA; Fabritz, S; Griss, R; Haas, D; Hiblot, J; Johnsson, K; Okun, JG; Roux, C; Xue, L; Yu, Q | 1 |
49 other study(ies) available for phenylalanine and nadp
| Article | Year |
|---|---|
On the regulation of tryptophan metabolism "via" kynurenine.
Topics: Animals; Hydrogen-Ion Concentration; Hydroxyindoleacetic Acid; Hydroxylation; Kynurenine; Mixed Function Oxygenases; NAD; NADP; Nicotinic Acids; ortho-Aminobenzoates; Phenylalanine; Rats; Serotonin; Solubility; Tryptophan; Xanthurenates | 1978 |
Role of the conserved active site residue tryptophan-24 of human dihydrofolate reductase as revealed by mutagenesis.
Topics: Allosteric Regulation; Apoenzymes; Binding Sites; Humans; Hydrogen; Hydrogen-Ion Concentration; Kinetics; Ligands; Mutation; NADP; Phenylalanine; Protein Denaturation; Tetrahydrofolate Dehydrogenase; Tetrahydrofolates; Tryptophan | 1991 |
Dihydrofolate reductase from Escherichia coli: probing the role of aspartate-27 and phenylalanine-137 in enzyme conformation and the binding of NADPH.
Topics: Aspartic Acid; Azides; Bacterial Proteins; Copper; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; NADP; Phenylalanine; Protein Binding; Protein Conformation; Tetrahydrofolate Dehydrogenase | 1990 |
Effects of conversion of phenylalanine-31 to leucine on the function of human dihydrofolate reductase.
Topics: Binding Sites; Folic Acid; Humans; Kinetics; Leucine; Methotrexate; Mutation; NADP; Phenylalanine; Recombinant Proteins; Structure-Activity Relationship; Tetrahydrofolate Dehydrogenase; Trimethoprim; X-Ray Diffraction | 1989 |
Dihydrofolate reductase. 1H resonance assignments and coenzyme-induced conformational changes.
Topics: Amino Acid Sequence; Histidine; Lacticaseibacillus casei; Magnetic Resonance Spectroscopy; Models, Molecular; NADP; Phenylalanine; Protein Conformation; Protons; Tetrahydrofolate Dehydrogenase; Tryptophan; Tyrosine | 1986 |
Probing the functional role of phenylalanine-31 of Escherichia coli dihydrofolate reductase by site-directed mutagenesis.
Topics: Amino Acids; Binding Sites; Deuterium; Escherichia coli; Folic Acid; Hydrogen-Ion Concentration; Kinetics; Mutation; NADP; Phenylalanine; Plasmids; Structure-Activity Relationship; Tetrahydrofolate Dehydrogenase; Tyrosine; Valine | 1987 |
Catalytic properties of NADPH-specific dihydropteridine reductase from bovine liver.
Topics: 2,6-Dichloroindophenol; Animals; Catalysis; Cattle; Dihydropteridine Reductase; Hydroxylation; Kinetics; Liver; NAD; NADH, NADPH Oxidoreductases; NADP; Phenylalanine; Thyroxine | 1986 |
Studies on the mechanisms of action of phenylalanine hydroxylase and its protein stimulator. I. Enzyme concentration dependence of the specific activity of phenylalanine hydroxylase due to a nonenzymatic step.
Topics: Animals; Catalysis; Centrifugation, Density Gradient; Enzyme Activation; Hydroxylation; Kinetics; Liver; Mathematics; Models, Chemical; Molecular Weight; NADP; Oxygen; Phenylalanine; Phenylalanine Hydroxylase; Propylene Glycols; Protein Binding; Proteins; Pteridines; Quinones; Rats; Scattering, Radiation | 1973 |
Tetrahydropterin oxidation without hydroxylation catalyzed by rat liver phenylalanine hydroxylase.
Topics: Animals; Azides; Carbon Isotopes; Catalase; Catalysis; Chymotrypsin; Free Radicals; Hydroxylation; Kinetics; Liver; Lysophosphatidylcholines; NADP; Oxidation-Reduction; Oxygen; Oxygen Consumption; Peroxidases; Phenylalanine; Phenylalanine Hydroxylase; Pteridines; Pyruvates; Rats; Sodium; Stereoisomerism; Tyrosine; Uncoupling Agents | 1973 |
Enzyme organization in the proline biosynthetic pathway of Escherichia coli.
Topics: Adenosine Triphosphate; Ammonia; Carbon Radioisotopes; Cell-Free System; Escherichia coli; Glucose; Glutamates; Imidazoles; Mutation; NADP; Oxidation-Reduction; Oxidoreductases; Phenylalanine; Phosphotransferases; Proline; Spectrophotometry; Ultracentrifugation | 1974 |
A new biosynthetic pathway to catecholamines via m-tyrosine.
Topics: Adrenal Glands; Animals; Benzyl Compounds; Brain; Carbon Radioisotopes; Catalysis; Catecholamines; Dihydroxyphenylalanine; Hydroxylation; In Vitro Techniques; Iron; Liver; Methyldopa; Methyltyrosines; Mice; Monoiodotyrosine; NADP; Phenylalanine; Phenylalanine Hydroxylase; Phosphates; Pterins; Rats; Structure-Activity Relationship; Tyrosine | 1974 |
Protein synthesis and aldosterone production.
Topics: Adrenal Glands; Aldosterone; Animals; Anti-Bacterial Agents; Chromatography, Paper; Corticosterone; Dactinomycin; Ethionine; Hexosephosphates; Hydrocortisone; In Vitro Techniques; Leucine; NADP; Nucleosides; Phenylalanine; Protein Biosynthesis; Puromycin; Rats | 1966 |
Inhibition of liver phenylalanine and tryptophan hydroxylating enzyme systems in vitro and in vivo.
Topics: Aminopterin; Animals; Brain Chemistry; Coumarins; Enzyme Induction; Enzymes; Flavonoids; In Vitro Techniques; Liver; Liver Extracts; Methyldopa; Mice; Mixed Function Oxygenases; NAD; NADP; Phenylacetates; Phenylalanine; Rats; Serotonin; Tryptophan | 1966 |
[The light-induced increase in the activity of NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase. IV. Influence on the intensity of the photosynthesis].
Topics: Alanine; Amino Acids; Chloramphenicol; Enzymes; Ethionine; Feedback; Light; Methionine; NADP; Phenylalanine; Photosynthesis; Plants | 1966 |
Metabolism of the phenylalanine hydroxylation cofactor.
Topics: Chromatography, Paper; Coenzymes; Hydrochloric Acid; Hydrogen-Ion Concentration; Kinetics; Liver; Mixed Function Oxygenases; NADP; Phenylalanine; Pterins; Spectrophotometry; Tetrahydrofolate Dehydrogenase; Ultraviolet Rays; Zinc | 1967 |
Flavensomycin, an inhibitor of enzyme reactions involving hydrogen transfer.
Topics: Alanine; Alcohol Oxidoreductases; Amino Acid Oxidoreductases; Antifungal Agents; Cytochromes; D-Amino-Acid Oxidase; Electron Transport; Flavin-Adenine Dinucleotide; Glucose Oxidase; Hexokinase; Isocitrate Dehydrogenase; L-Lactate Dehydrogenase; Leucine; NAD; NADP; Oxidoreductases; Penicillium; Phenylalanine; Pyruvates | 1967 |
[On the metabolism and mechanism of action of estrogens. 8. The biogenesis and metabolism of 2-hydroxyestrone in relation to the formation of protein-bound and water soluble estrone metabolites and to NADPH oxidation in rat liver microsomes].
Topics: Aminopterin; Animals; Carbon Isotopes; Cysteine; Estrone; Female; Folic Acid; Glutathione; Humans; Kinetics; Liver; Male; Microsomes; NADP; Oxidation-Reduction; Phenylalanine; Phosphates; Protein Binding; Pteridines; Rats; Steroids | 1966 |
Effect of phenobarbital treatment on the activities of NADPH-dependent enzymes of liver microsomes in fasting or sucrose-fed rats.
Topics: Aminopyrine; Aniline Compounds; Animals; Benzoates; Carbon Isotopes; Female; Liver; Male; Microsomes; Mixed Function Oxygenases; NADP; Oxidoreductases; Phenobarbital; Phenylalanine; Rats; Starvation; Sucrose | 1967 |
The role of pteridine cofactors in mixed function oxidases.
Topics: Adrenal Glands; Animals; Cattle; Liver; Mixed Function Oxygenases; NADP; Phenylalanine; Pteridines; Rats; Tyrosine | 1968 |
The formation of 3,4-dihydroxy-L-phenylalanine from L-meta-tyrosine by rat liver and beef adrenal medulla.
Topics: Adrenal Glands; Amino Acids; Animals; Aromatic Amino Acid Decarboxylase Inhibitors; Autoanalysis; Cattle; Chemical Precipitation; Chromatography, Ion Exchange; Cresols; Depression, Chemical; Dihydroxyphenylalanine; Ethanol; Female; Fluorescence; Hydroxylamines; Isomerism; Liver; Mixed Function Oxygenases; NADP; Phenylalanine; Pteridines; Quaternary Ammonium Compounds; Rats; Stimulation, Chemical; Sulfates; Tyrosine | 1971 |
[Hydroxylation of phenylalanine by Hydrogenomonas eutropha H 16].
Topics: Cell-Free System; Chromatography, Gel; Enzyme Induction; Mixed Function Oxygenases; NAD; NADP; Phenylalanine; Phenylalanine Hydroxylase; Phenylpyruvic Acids; Pseudomonas; Tryptophan; Tyrosine | 1972 |
Arogenate (pretyrosine) pathway of tyrosine and phenylalanine biosynthesis in Pseudomonas aureofaciens ATCC 15926.
Topics: Amino Acids, Dicarboxylic; Cyclohexenes; NAD; NADP; Oxidoreductases; Phenylalanine; Prephenate Dehydrogenase; Pseudomonas; Tyrosine | 1982 |
Critical role of phenylalanine 34 of human dihydrofolate reductase in substrate and inhibitor binding and in catalysis.
Topics: Ammonium Sulfate; Catalysis; Chemical Precipitation; Enzyme Stability; Folic Acid; Humans; Hydrogen-Ion Concentration; Kinetics; Methotrexate; Mutagenesis, Site-Directed; NADP; Phenylalanine; Structure-Activity Relationship; Tetrahydrofolate Dehydrogenase | 1994 |
Methotrexate-resistant variants of human dihydrofolate reductase. Effects of Phe31 substitutions.
Topics: Amino Acid Sequence; Crystallography, X-Ray; Drug Resistance; Enzyme Stability; Genetic Therapy; Genetic Variation; Humans; Kinetics; Methotrexate; Models, Structural; Models, Theoretical; Mutagenesis, Site-Directed; NADP; Phenylalanine; Protein Conformation; Protein Denaturation; Protein Folding; Recombinant Proteins; Tetrahydrofolate Dehydrogenase | 1994 |
Mutagenesis at a highly conserved phenylalanine in cytochrome P450 2E1 affects heme incorporation and catalytic activity.
Topics: Amino Acid Sequence; Animals; Catalysis; Conserved Sequence; Cytochrome P-450 CYP2E1; Cytochrome P-450 Enzyme System; Escherichia coli; Heme; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NADP; Oxidoreductases, N-Demethylating; Phenylalanine; Rabbits; Structure-Activity Relationship | 1994 |
How do mutations at phenylalanine-153 and isoleucine-155 partially suppress the effects of the aspartate-27-->serine mutation in Escherichia coli dihydrofolate reductase?
Topics: Bacterial Proteins; DNA Mutational Analysis; Escherichia coli; Hydrogen Bonding; Hydrogen-Ion Concentration; Isoleucine; Kinetics; Models, Molecular; Mutation; NADP; Phenylalanine; Protein Structure, Secondary; Structure-Activity Relationship; Tetrahydrofolate Dehydrogenase | 1993 |
A large compressibility change of protein induced by a single amino acid substitution.
Topics: Aspartate Aminotransferases; Aspartic Acid; Escherichia coli; Glutamic Acid; Glycine; Linear Models; NADP; Phenylalanine; Point Mutation; Proteins; Pyridoxal Phosphate; Tetrahydrofolate Dehydrogenase; Valine | 1996 |
An active site substitution, F87V, converts cytochrome P450 BM-3 into a regio- and stereoselective (14S,15R)-arachidonic acid epoxygenase.
Topics: Animals; Bacterial Proteins; Binding Sites; Cytochrome P-450 CYP2J2; Cytochrome P-450 Enzyme System; Gas Chromatography-Mass Spectrometry; Mixed Function Oxygenases; Models, Molecular; Mutagenesis, Site-Directed; NADP; NADPH-Ferrihemoprotein Reductase; Oxygenases; Phenylalanine; Stereoisomerism; Valine | 1997 |
A single amino acid substitution in Staphylococcus aureus dihydrofolate reductase determines trimethoprim resistance.
Topics: Binding Sites; Chromosomes, Bacterial; Crystallography, X-Ray; Humans; Models, Molecular; Molecular Conformation; NADP; Phenylalanine; Point Mutation; Protein Conformation; Staphylococcus aureus; Tetrahydrofolate Dehydrogenase; Trimethoprim; Trimethoprim Resistance; Tyrosine | 1997 |
Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability.
Topics: 4-Hydroxybenzoate-3-Monooxygenase; Amino Acid Substitution; Arginine; Binding Sites; Crystallization; Crystallography, X-Ray; Enzyme Stability; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Kinetics; NADP; Phenylalanine; Protein Conformation; Pseudomonas fluorescens; Spectrum Analysis; Temperature; Time Factors | 1999 |
Effects of single-tryptophan mutations on R67 dihydrofolate reductase.
Topics: Binding Sites; Chromatography, Gel; Circular Dichroism; Energy Transfer; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; NADP; Phenylalanine; Protein Folding; Quantum Theory; R Factors; Spectrometry, Fluorescence; Tetrahydrofolate Dehydrogenase; Tryptophan | 2000 |
Aromatic residues and neighboring Arg414 in the (6R)-5,6,7, 8-tetrahydro-L-biopterin binding site of full-length neuronal nitric-oxide synthase are crucial in catalysis and heme reduction with NADPH.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Binding Sites; Biopterins; Catalysis; Dimerization; Drosophila; Glutamine; Heme; Humans; Hydrogen Bonding; Leucine; Mice; Models, Molecular; Molecular Sequence Data; NADP; Nitric Oxide Synthase; Nitric Oxide Synthase Type I; Oxidation-Reduction; Phenylalanine; Rats; Spectrophotometry, Atomic; Structure-Activity Relationship; Tryptophan | 2000 |
Rhodococcus L-phenylalanine dehydrogenase: kinetics, mechanism, and structural basis for catalytic specificity.
Topics: Amino Acid Oxidoreductases; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors; Hydrogen; Hydrogen-Ion Concentration; Kinetics; Lactates; Ligands; Models, Molecular; Molecular Sequence Data; NAD; NADP; Phenylalanine; Phenylpropionates; Protein Conformation; Rhodococcus; Stereoisomerism; Structure-Activity Relationship; Substrate Specificity | 2000 |
Critical role of the residue size at position 87 in H2O2- dependent substrate hydroxylation activity and H2O2 inactivation of cytochrome P450BM-3.
Topics: Amino Acid Substitution; Bacterial Proteins; Cytochrome P-450 Enzyme System; Enzyme Activation; Fatty Acids; Hydrogen Peroxide; Hydroxylation; Mixed Function Oxygenases; Mutagenesis, Site-Directed; Mutation; NADP; NADPH-Ferrihemoprotein Reductase; Phenylalanine; Substrate Specificity | 2001 |
Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart NADP-dependent isocitrate dehydrogenase.
Topics: Amino Acid Sequence; Animals; Binding Sites; Circular Dichroism; Escherichia coli; Ferrous Compounds; Glutamine; Histidine; Hydrogen-Ion Concentration; Hydrolysis; Isocitrate Dehydrogenase; Isocitrates; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Myocardium; NADP; Phenylalanine; Protein Structure, Secondary; Recombinant Proteins; Substrate Specificity; Swine | 2002 |
Oxidative stress in a phenylketonuria animal model.
Topics: Animals; Brain; Catalase; Chromatography, High Pressure Liquid; Disease Models, Animal; Erythrocytes; Glucosephosphate Dehydrogenase; Glutathione; Hydrogen Peroxide; Lipid Peroxidation; Malondialdehyde; Mice; Mice, Knockout; NADP; Oxidation-Reduction; Oxidative Stress; Oxygen; Phenylalanine; Phenylketonurias | 2002 |
Optimizing an artificial metabolic pathway: engineering the cofactor specificity of Corynebacterium 2,5-diketo-D-gluconic acid reductase for use in vitamin C biosynthesis.
Topics: Alanine; Amino Acid Substitution; Ascorbic Acid; Binding Sites; Corynebacterium; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Gluconates; Glycine; Kinetics; Mutagenesis, Site-Directed; NAD; NADP; Phenylalanine; Recombinant Fusion Proteins; Sugar Alcohol Dehydrogenases; Thermodynamics; Tyrosine | 2002 |
Use of kinetic isotope effects to delineate the role of phenylalanine 87 in P450(BM-3).
Topics: Amino Acid Substitution; Bacillus megaterium; Bacterial Proteins; Biphenyl Compounds; Catalytic Domain; Cytochrome P-450 Enzyme System; Deuterium; Kinetics; Mixed Function Oxygenases; NADP; NADPH-Ferrihemoprotein Reductase; Phenylalanine; Substrate Specificity; Xylenes | 2002 |
Glutamate-115 renders specificity of human 11beta-hydroxysteroid dehydrogenase type 2 for the cofactor NAD+.
Topics: 11-beta-Hydroxysteroid Dehydrogenase Type 2; Amino Acid Sequence; Aspartic Acid; Binding Sites; Catalytic Domain; Computer Simulation; Glutamates; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; NADP; Phenylalanine; Protein Conformation; Sequence Homology, Amino Acid | 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 |
STUDIES ON THE STRUCTURE OF THE PRIMARY OXIDATION PRODUCT FORMED FROM TETRAHYDROPTERIDINES DURING PHENYLALAMINE HYDROXYLATION.
Topics: Fluorescence; Freeze Drying; Hydroxylation; Mixed Function Oxygenases; NADP; Oxidation-Reduction; Phenylalanine; Proteins; Pteridines; Pterins; Research; Tritium | 1964 |
THE INFLUENCE OF PHENOBARBITAL ADMINISTRATION UPON THE "SOLUBLE" NADP-REQUIRING ENZYMES IN LIVER.
Topics: Aminopyrine; Benzopyrenes; Citrates; Diphenhydramine; Ethionine; Fluorouracil; Gluconates; Hexosephosphates; Isocitrate Dehydrogenase; Liver; Mercaptopurine; Methylcholanthrene; NADP; Oxidoreductases; Pharmacology; Phenobarbital; Phenylalanine; Rats; Research; Uracil | 1964 |
PREPARATION OF PREPHENIC ACID AND ITS CONVERSION TO PHENYLALANINE AND TYROSINE BY PLANT ENZYMES.
Topics: Autoanalysis; Barium; Cyclohexanecarboxylic Acids; Cyclohexenes; Escherichia coli; Fermentation; Glutamates; Infrared Rays; Ion Exchange Resins; NADP; Peptones; Phenylalanine; Phenylpyruvic Acids; Plants, Edible; Proteins; Research; Transaminases; Tyrosine; Yeasts | 1964 |
Crystal structures of the multispecific 17beta-hydroxysteroid dehydrogenase type 5: critical androgen regulation in human peripheral tissues.
Topics: 17-Hydroxysteroid Dehydrogenases; 3-Hydroxysteroid Dehydrogenases; Aldo-Keto Reductase Family 1 Member C3; Androgens; Androstenedione; Binding Sites; Crystallography, X-Ray; Humans; Hydroxyprostaglandin Dehydrogenases; Male; Models, Molecular; NADP; Phenylalanine; Prostate; Protein Conformation; Testosterone | 2004 |
Role of methionine-13 in the catalytic mechanism of 6-phosphogluconate dehydrogenase from sheep liver.
Topics: Amino Acid Sequence; Animals; Catalysis; Circular Dichroism; Cysteine; Deuterium Exchange Measurement; Glutamine; Kinetics; Liver; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; NADP; Phenylalanine; Phosphogluconate Dehydrogenase; Sheep | 2005 |
An enzymatic fluorimetric assay for glucose-6-phosphate: application in an in vitro Warburg-like effect.
Topics: Enzyme Assays; Fluorometry; Glucose-6-Phosphate; Glucosephosphate Dehydrogenase; Humans; Jurkat Cells; NADP; Oxazines; Phenylalanine | 2009 |
Simultaneous involvement of a tungsten-containing aldehyde:ferredoxin oxidoreductase and a phenylacetaldehyde dehydrogenase in anaerobic phenylalanine metabolism.
Topics: Aldehyde Oxidoreductases; Anaerobiosis; Coenzymes; Escherichia coli Proteins; Metabolic Networks and Pathways; NAD; NADP; Nitrates; Oxidation-Reduction; Phenylacetates; Phenylalanine; Rhodocyclaceae; Tungsten | 2014 |
Delineating the reaction mechanism of reductase domains of Nonribosomal Peptide Synthetases from mycobacteria.
Topics: Bacterial Proteins; Binding Sites; Binding, Competitive; Calorimetry; Catalytic Domain; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Structure; Mutation; Mycobacterium smegmatis; Mycobacterium tuberculosis; NADP; Niacinamide; Peptide Synthases; Phenylalanine; Protein Binding; Protein Structure, Tertiary; Scattering, Small Angle; Thermodynamics; Tyrosine; X-Ray Diffraction | 2014 |
Semisynthetic sensor proteins enable metabolic assays at the point of care.
Topics: Bioluminescence Resonance Energy Transfer Techniques; Biosensing Techniques; Blood Glucose; Escherichia coli Proteins; Glutamic Acid; Humans; Monitoring, Physiologic; NADP; Oxidation-Reduction; Phenylalanine; Phenylketonurias; Point-of-Care Testing; Tetrahydrofolate Dehydrogenase | 2018 |