| EC |
1.1.1.35 |
| Accepted name: |
3-hydroxyacyl-CoA dehydrogenase |
| Reaction: |
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+ |
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| Other name(s): |
β-hydroxyacyl dehydrogenase; β-keto-reductase; 3-keto reductase; 3-hydroxyacyl coenzyme A dehydrogenase; β-hydroxyacyl-coenzyme A synthetase; β-hydroxyacylcoenzyme A dehydrogenase; β-hydroxybutyrylcoenzyme A dehydrogenase; 3-hydroxyacetyl-coenzyme A dehydrogenase; L-3-hydroxyacyl coenzyme A dehydrogenase; L-3-hydroxyacyl CoA dehydrogenase; β-hydroxyacyl CoA dehydrogenase; 3β-hydroxyacyl coenzyme A dehydrogenase; 3-hydroxybutyryl-CoA dehydrogenase; β-ketoacyl-CoA reductase; β-hydroxy acid dehydrogenase; 3-L-hydroxyacyl-CoA dehydrogenase; 3-hydroxyisobutyryl-CoA dehydrogenase; 1-specific DPN-linked β-hydroxybutyric dehydrogenase |
| Systematic name: |
(S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase |
| Comments: |
Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacyl-hydrolipoate. Some enzymes act, more slowly, with NADP+. Broad specificity to acyl chain-length (cf. EC 1.1.1.211 [long-chain-3-hydroxyacyl-CoA dehydrogenase]). |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-40-4 |
| References: |
| 1. |
Hillmer, P. and Gottschalk, G. Solubilization and partial characterisation of particulate dehydrogenases from Clostridium kluyveri. Biochim. Biophys. Acta 334 (1974) 12–23. |
| 2. |
Lehninger, A.L. and Greville, G.D. The enzymatic oxidation of d- and l-β-hydroxybutyrate. Biochim. Biophys. Acta 12 (1953) 188–202. [DOI] [PMID: 13115428] |
| 3. |
Stern, J.R. Crystalline β-hydroxybutyrate dehydrogenase from pig heart. Biochim. Biophys. Acta 26 (1957) 448–449. [DOI] [PMID: 13499396] |
| 4. |
Wakil, S.J., Green, D.E., Mii, S. and Mahler, H.R. Studies on the fatty acid oxidizing system of animal tissues. VI. β-Hydroxyacyl coenzyme A dehydrogenase. J. Biol. Chem. 207 (1954) 631–638. [PMID: 13163047] |
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| [EC 1.1.1.35 created 1961] |
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