alpha-ketoisovalerate has been researched along with acetyl coenzyme a in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (66.67) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 1 (33.33) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Kolsaker, P; Nesbakken, T; Ormerod, J | 1 |
| Corkey, BE; Martin-Requero, A; Walajtys-Rode, E; Williams, RJ; Williamson, JR | 1 |
| Baker, EN; Baker, HM; Bulloch, EM; Huisman, FH; Koon, N; Parker, EJ; Squire, CJ | 1 |
3 other study(ies) available for alpha-ketoisovalerate and acetyl coenzyme a
| Article | Year |
|---|---|
Mechanism of biosynthesis of 2-oxo-3-methylvalerate in Chlorobium vibrioforme.
Topics: Acetyl Coenzyme A; Bacteria; Chemical Phenomena; Chemistry; Hemiterpenes; Keto Acids; Magnetic Resonance Spectroscopy | 1988 |
Regulation of the branched chain alpha-ketoacid pathway in liver.
Topics: 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide); Acetoacetates; Acetyl Coenzyme A; Acyl Coenzyme A; Animals; Carbon Dioxide; Citric Acid Cycle; Hemiterpenes; Keto Acids; Ketone Oxidoreductases; Liver; Male; Multienzyme Complexes; Oleic Acid; Oleic Acids; Propionates; Rats; Rats, Inbred Strains | 1982 |
Removal of the C-terminal regulatory domain of α-isopropylmalate synthase disrupts functional substrate binding.
Topics: 2-Isopropylmalate Synthase; Acetyl Coenzyme A; Binding Sites; Catalysis; Catalytic Domain; Crystallography, X-Ray; Hemiterpenes; Keto Acids; Kinetics; Mycobacterium tuberculosis; Neisseria meningitidis; Substrate Specificity | 2012 |