pyridoxal phosphate has been researched along with diacetyl in 11 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 9 (81.82) | 18.7374 |
| 1990's | 2 (18.18) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Hemmilä, IA; Mäntsälä, PI | 1 |
| Andreone, P; Frerman, FE; Mielke, D | 1 |
| Chirikjian, JG; Lee, YH | 1 |
| Bellini, T; Dallocchio, F; Rippa, M; Signorini, M | 1 |
| Kazarinoff, MN; Snell, EE | 1 |
| Chatagner, F; Pierre, Y | 1 |
| Nakagawa, H; Ogura, N; Sato, T; Sato, Y; Shiraishi, N | 1 |
| Csermely, P; Dux, L; Martonosi, A; Mullner, N; Varga, S | 1 |
| Kato, M; Maruhashi, J; Oomura, Y | 1 |
| Gracy, RW; Lu, HS; Talent, JM | 1 |
| Bazaes, S; Cardemil, E; Goldie, H; Jabalquinto, AM; Silva, R | 1 |
11 other study(ies) available for pyridoxal phosphate and diacetyl
| Article | Year |
|---|---|
Inactivation of glutamate dehydrogenase and glutamate synthase from Bacillus megaterium by phenylglyoxal, butane-2,3-dione and pyridoxal 5'-phosphate.
Topics: Aldehydes; Arginine; Bacillus megaterium; Binding Sites; Butanones; Diacetyl; Glutamate Dehydrogenase; Glutamate Synthase; Glyoxal; Kinetics; NADP; Pyridoxal Phosphate; Transaminases | 1978 |
Reaction of pyridoxal 5'-phosphate with Escherichia coli CoA transferase: evidence for an essential lysine residue.
Topics: Acetoacetates; Acetyl-CoA C-Acyltransferase; Acyltransferases; Binding Sites; Coenzyme A; Diacetyl; Escherichia coli; Kinetics; Lysine; Pyridoxal Phosphate | 1977 |
Sequence-specific endonuclease Bgl I. Modification of lysine and arginine residues of the homogeneous enzyme.
Topics: Arginine; Bacillus; Deoxyribonucleases; Diacetyl; Endonucleases; Kinetics; Lysine; Magnesium; Molecular Weight; Pyridoxal Phosphate | 1979 |
The active site of 6-phosphogluconate dehydrogenase. A phosphate binding site and its surroundings.
Topics: Arginine; Arsenates; Binding Sites; Candida; Diacetyl; Dithionitrobenzoic Acid; Histidine; Lysine; Phosphates; Phosphogluconate Dehydrogenase; Pyridoxal Phosphate; Sulfhydryl Compounds | 1978 |
D-Serine dehydratase from Escherichia coli. Essential arginine residue at the pyridoxal 5'-phosphate binding site.
Topics: Apoenzymes; Arginine; Binding Sites; Diacetyl; Escherichia coli; Kinetics; L-Serine Dehydratase; Protein Binding; Pyridoxal Phosphate | 1976 |
Functional arginine in the active center of rat liver cystathionase.
Topics: Animals; Arginine; Binding Sites; Binding, Competitive; Cystathionine gamma-Lyase; Cysteine; Diacetyl; Homoserine; Liver; Lyases; Pyridoxal Phosphate; Rats | 1977 |
Arginine and lysine residues as NADH-binding sites in NADH-nitrate reductase from spinach.
Topics: Amino Acid Sequence; Arginine; Binding Sites; Diacetyl; Humans; Lysine; Molecular Sequence Data; NAD; NADH, NADPH Oxidoreductases; Nitrate Reductase (NADH); Nitrate Reductases; Phenylglyoxal; Plants; Pyridoxal Phosphate; Sequence Homology, Nucleic Acid | 1992 |
Effect of chemical modification on the crystallization of Ca2+-ATPase in sarcoplasmic reticulum.
Topics: Animals; Calcium; Calcium-Transporting ATPases; Crystallization; Detergents; Diacetyl; Fluorescamine; Fluorescein-5-isothiocyanate; Fluoresceins; Membrane Proteins; Metals, Rare Earth; Phenylglyoxal; Phospholipases; Polymers; Protein Conformation; Pyridoxal Phosphate; Rabbits; Sarcoplasmic Reticulum; Sulfhydryl Reagents; Thiocyanates; Vanadates; Vanadium | 1987 |
Effects of chemical modification on the L-glutamate receptors on the Onchidium neuron.
Topics: Animals; Diacetyl; Dithiothreitol; Ethylmaleimide; Glutamates; Glutamic Acid; Isoflurophate; Mollusca; Molybdenum; Neurons; Pyridoxal Phosphate; Quinolines; Receptors, Cell Surface; Receptors, Glutamate; Receptors, Neurotransmitter; Structure-Activity Relationship; Trinitrobenzenesulfonic Acid | 1983 |
Chemical modification of critical catalytic residues of lysine, arginine, and tryptophan in human glucose phosphate isomerase.
Topics: Affinity Labels; Arginine; Bromosuccinimide; Circular Dichroism; Cyclohexanones; Diacetyl; Female; Glucose-6-Phosphate Isomerase; Humans; Kinetics; Lysine; Molecular Weight; Placenta; Pregnancy; Protein Binding; Protein Conformation; Pyridoxal Phosphate; Tryptophan | 1981 |
Reactivity of cysteinyl, arginyl, and lysyl residues of Escherichia coli phosphoenolpyruvate carboxykinase against group-specific chemical reagents.
Topics: Arginine; Binding Sites; Cysteine; Diacetyl; Escherichia coli; Glyoxal; Kinetics; Lysine; Phosphoenolpyruvate Carboxykinase (GTP); Pyrenes; Pyridoxal Phosphate; Sulfhydryl Reagents | 1993 |