nad has been researched along with 3-hydroxybutyryl-coenzyme a in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (25.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 3 (75.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Ghayourmanesh, S; Kumar, S | 1 |
| Besra, GS; Bhatt, A; Brown, AK; Singh, A; Taylor, RC | 1 |
| Eggers, J; Steinbüchel, A | 1 |
| Ahn, JW; Chang, JH; Kim, EJ; Kim, J; Kim, KJ; Kim, YJ | 1 |
4 other study(ies) available for nad and 3-hydroxybutyryl-coenzyme a
| Article | Year |
|---|---|
Synthesis of acetoacetyl-CoA by bovine mammary fatty acid synthase.
Topics: 3-Hydroxyacyl CoA Dehydrogenases; Acetyl Coenzyme A; Acyl Coenzyme A; Animals; Cattle; Coenzyme A; Fatty Acid Synthases; Female; Kinetics; Lactation; Mammary Glands, Animal; NAD; Oxidation-Reduction; Pregnancy; Pyrones | 1981 |
Characterization of a beta-hydroxybutyryl-CoA dehydrogenase from Mycobacterium tuberculosis.
Topics: 3-Hydroxyacyl CoA Dehydrogenases; Acyl Coenzyme A; Amino Acid Sequence; Bacterial Proteins; Enzyme Stability; Molecular Sequence Data; Mutation; Mycobacterium tuberculosis; NAD; Sequence Alignment | 2010 |
Poly(3-hydroxybutyrate) degradation in Ralstonia eutropha H16 is mediated stereoselectively to (S)-3-hydroxybutyryl coenzyme A (CoA) via crotonyl-CoA.
Topics: Acyl Coenzyme A; Bacterial Proteins; Carboxylic Ester Hydrolases; Chromatography, Liquid; Cupriavidus necator; DNA-Binding Proteins; Escherichia coli; Gene Deletion; Hydroxybutyrates; Mass Spectrometry; Metabolic Engineering; Metabolic Networks and Pathways; NAD; Polyesters | 2013 |
Crystal structure of (S)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium butyricum and its mutations that enhance reaction kinetics.
Topics: 1-Butanol; 3-Hydroxyacyl CoA Dehydrogenases; Acetyl Coenzyme A; Acyl Coenzyme A; Amino Acid Sequence; Clostridium butyricum; Crystallography, X-Ray; Kinetics; Models, Molecular; Molecular Sequence Data; Mutant Proteins; Mutation, Missense; NAD; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Interaction Domains and Motifs; Protein Multimerization | 2014 |