diacetyl and nad
diacetyl has been researched along with nad in 24 studies
Research
Studies (24)
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 12 (50.00) | 18.7374 |
| 1990's | 6 (25.00) | 18.2507 |
| 2000's | 2 (8.33) | 29.6817 |
| 2010's | 4 (16.67) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
Authors
| Authors | Studies |
|---|---|
| Afolayan, A; Ingulli, J; Levy, HR | 1 |
| Aspiiants, RA; Benkevich, NV; Nagradova, NK | 1 |
| Colman, RF; Hayman, S | 1 |
| Bragg, PD; Homyk, M | 1 |
| Butterworth, PJ; Woodroofe, MN | 1 |
| Nakagawa, H; Ogura, N; Sato, T; Sato, Y; Shiraishi, N | 1 |
| Dekker, EE; Epperly, BR | 1 |
| Koide, S; Matsuzawa, H; Miyazawa, T; Ohta, T; Yokoyama, S | 1 |
| Asryants, RA; Douzhenkova, IV; Nagradova, NK | 1 |
| Asriiants, RA; Benkevich, NV; Nagradova, NK | 1 |
| Ashmarina, LI; Asryants, RA; Muronetz, VI; Nagradova, NK | 1 |
| Berezin, IV; Egorov, AM; Popov, VO; Tishkov, VI | 1 |
| Kusaka, T; Shimakata, T | 1 |
| Branlant, G; Corbier, C; Michels, S; Wonacott, AJ | 1 |
| Ebus, JP; Stienen, GJ | 1 |
| Boumerdassi, H; Corrieu, G; Desmazeaud, M; Monnet, C | 1 |
| Diviès, C; Huang, DQ; Phalip, V; Prévost, H; Schmitt, P; Vasseur, C | 1 |
| de Vos, WM; Hugenholtz, J; Kleerebezem, M; Lopez de Felipe, F | 1 |
| Grotyohann, LW; Scaduto, RC | 1 |
| Jyoti, BD; Suresh, AK; Venkatesh, KV | 1 |
| Guo, T; Hu, S; Kong, J; Zhang, C; Zhang, L | 1 |
| Gao, C; Li, L; Ma, C; Tao, F; Wang, Y; Xu, P | 1 |
| Gao, X; Li, S; Liu, L; Xu, N | 1 |
| Huang, M; Shao, J; Song, Q; Ying, X; Yu, M | 1 |
Other Studies
24 other study(ies) available for diacetyl and nad
| Article | Year |
|---|---|
Identification of essential arginine residues in glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides.
Topics: Amino Acids; Arginine; Butanones; Diacetyl; Fluorescence; Glucosephosphate Dehydrogenase; Glucosephosphates; Kinetics; Leuconostoc; NAD; NADP; Scattering, Radiation | 1977 |
[Cooperativity of the active centers of D-glyceraldehyde-3-phosphate dehydrogenase revealed by the arginine residue modification method].
Topics: Arginine; Binding Sites; Diacetyl; Enzyme Activation; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; NAD; Substrate Specificity | 1978 |
Effect of arginine modification on the catalytic activity and allosteric activation by adenosine diphosphate of the diphosphopyridine nucleotide specific isocitrate dehydrogenase of pig heart.
Topics: Adenosine Diphosphate; Allosteric Regulation; Animals; Arginine; Butanones; Diacetyl; Enzyme Activation; Isocitrate Dehydrogenase; Kinetics; Myocardium; NAD; Swine | 1978 |
Photooxidation of NADH by 2,3-butanedione: a potential source of error in studies on active site arginyl residues.
Topics: Arginine; Butanones; Diacetyl; Light; NAD; Oxidation-Reduction | 1979 |
Evidence for the importance of arginine residues in pig kidney alkaline phosphatase.
Topics: Alkaline Phosphatase; Animals; Arginine; Diacetyl; Glyoxal; Kidney Cortex; Kinetics; Ligands; NAD; Swine | 1979 |
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 |
Inactivation of Escherichia coli L-threonine dehydrogenase by 2,3-butanedione. Evidence for a catalytically essential arginine residue.
Topics: Alcohol Oxidoreductases; Arginine; Binding Sites; Butanones; Catalysis; Cyclohexanones; Diacetyl; Escherichia coli; Kinetics; NAD; Pentanones; Phenylglyoxal | 1989 |
Conformation of NAD+ bound to allosteric L-lactate dehydrogenase activated by chemical modification.
Topics: Allosteric Regulation; Allosteric Site; Arginine; Butanones; Diacetyl; Fructosediphosphates; Hexosediphosphates; Kinetics; L-Lactate Dehydrogenase; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Conformation; NAD; Thermus | 1989 |
D-glyceraldehyde-3-phosphate dehydrogenase subunit cooperativity studied using immobilized enzyme forms.
Topics: Allosteric Regulation; Animals; Diacetyl; Enzymes, Immobilized; Glyceraldehyde 3-Phosphate; Glyceraldehyde-3-Phosphate Dehydrogenases; Hot Temperature; Kinetics; Macromolecular Substances; Muscles; NAD; Rabbits; Structure-Activity Relationship; Sulfhydryl Compounds | 1988 |
[Modification of arginine residues of glyceraldehyde 3-phosphate dehydrogenase. The enzyme from rat and rabbit skeletal muscles].
Topics: Animals; Arginine; Butanones; Diacetyl; Glyceraldehyde-3-Phosphate Dehydrogenases; Kinetics; Macromolecular Substances; Muscles; NAD; Rabbits; Rats; Species Specificity | 1983 |
Use of immobilized enzymatically active monomers of glyceraldehyde-3-phosphate dehydrogenase to investigate subunit cooperativity in the oligomeric enzyme.
Topics: Animals; Arginine; Diacetyl; Enzymes, Immobilized; Glyceraldehyde-3-Phosphate Dehydrogenases; Macromolecular Substances; NAD; Protein Conformation; Rats; Saccharomyces cerevisiae | 1980 |
Study of the role of arginine residues in bacterial formate dehydrogenase.
Topics: Alcaligenes; Aldehyde Oxidoreductases; Amino Acids; Arginine; Azides; Diacetyl; Formate Dehydrogenases; Formates; NAD | 1981 |
Purification and characterization of 2-enoyl-CoA reductase of Mycobacterium smegmatis.
Topics: Diacetyl; Fatty Acid Desaturases; Molecular Weight; Mycobacterium; NAD; Phenylglyoxal | 1981 |
Characterization of the two anion-recognition sites of glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus by site-directed mutagenesis and chemical modification.
Topics: Anions; Binding Sites; Crystallization; Diacetyl; Geobacillus stearothermophilus; Glyceraldehyde-3-Phosphate Dehydrogenases; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; NAD; Phosphates | 1994 |
Effects of 2,3-butanedione monoxime on cross-bridge kinetics in rat cardiac muscle.
Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Diacetyl; Isometric Contraction; Kinetics; Male; Models, Cardiovascular; Myocardial Contraction; Myocardium; NAD; Rats | 1996 |
Isolation and properties of Lactococcus lactis subsp. lactis biovar diacetylactis CNRZ 483 mutants producing diacetyl and acetoin from glucose.
Topics: Acetoin; Base Sequence; Diacetyl; DNA Primers; Glucose; Kinetics; L-Lactate Dehydrogenase; Lactococcus lactis; Mutation; NAD | 1997 |
Diacetyl and acetoin production from the co-metabolism of citrate and xylose by Leuconostoc mesenteroides subsp. mesenteroides.
Topics: Acetoin; Citric Acid; Diacetyl; Leuconostoc; NAD; Xylose | 1997 |
Cofactor engineering: a novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase.
Topics: Acetoin; Aerobiosis; Cloning, Molecular; Diacetyl; Fermentation; Flavin-Adenine Dinucleotide; Gene Expression Regulation, Bacterial; Genetic Engineering; Glucose; Lactococcus lactis; Multienzyme Complexes; NAD; NADH, NADPH Oxidoreductases; Nisin; Promoter Regions, Genetic; Recombinant Proteins; Streptococcus mutans | 1998 |
2,3-butanedione monoxime unmasks Ca(2+)-induced NADH formation and inhibits electron transport in rat hearts.
Topics: Adenine Nucleotides; Adenosine Diphosphate; Animals; Calcium; Diacetyl; Electron Transport; Energy Metabolism; Heart; In Vitro Techniques; Mitochondria, Heart; Myocardium; NAD; Oxygen Consumption; Perfusion; Rats; Submitochondrial Particles | 2000 |
Effect of preculturing conditions on growth of Lactobacillus rhamnosus on medium containing glucose and citrate.
Topics: Acetoin; Biomass; Citric Acid; Culture Media; Diacetyl; Glucose; Lactobacillus; Multienzyme Complexes; NAD; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Oxygen | 2004 |
Fine tuning of the lactate and diacetyl production through promoter engineering in Lactococcus lactis.
Topics: Base Sequence; Cell Survival; Diacetyl; Genetic Engineering; Hydrogen Peroxide; Intracellular Space; Lactic Acid; Lactococcus lactis; Molecular Sequence Data; Multienzyme Complexes; NAD; NADH, NADPH Oxidoreductases; Promoter Regions, Genetic | 2012 |
Engineering of cofactor regeneration enhances (2S,3S)-2,3-butanediol production from diacetyl.
Topics: Butylene Glycols; Catalysis; Diacetyl; Escherichia coli; Formate Dehydrogenases; Gene Expression; Genes, Bacterial; Genes, Fungal; NAD | 2013 |
Metabolic engineering of Candida glabrata for diacetyl production.
Topics: Acetoin Dehydrogenase; Acetolactate Synthase; Alcohol Oxidoreductases; Candida glabrata; Carbon Cycle; Culture Media; Decarboxylation; Diacetyl; Fermentation; Gene Deletion; Iron; Lactates; Metabolic Engineering; Metabolic Networks and Pathways; NAD; Niacin; Pyruvic Acid; Thiamine | 2014 |
Characterization of a (2R,3R)-2,3-Butanediol Dehydrogenase from Rhodococcus erythropolis WZ010.
Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Bacterial Proteins; Butylene Glycols; Cloning, Molecular; Diacetyl; Hydrogen-Ion Concentration; Kinetics; Molecular Conformation; Molecular Sequence Data; NAD; Rhodococcus; Substrate Specificity; Temperature | 2015 |