| EC |
1.2.1.10 |
| Accepted name: |
acetaldehyde dehydrogenase (acetylating) |
| Reaction: |
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+ |
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For diagram of cinnamate catabolism, click here and for diagram of 3-phenylpropanoate catabolism, click here |
| Other name(s): |
aldehyde dehydrogenase (acylating); ADA; acylating acetaldehyde dehyrogenase; DmpF |
| Systematic name: |
acetaldehyde:NAD+ oxidoreductase (CoA-acetylating) |
| Comments: |
Also acts, more slowly, on glycolaldehyde, propanal and butanal. In Pseudomonas species, this enzyme forms part of a bifunctional enzyme with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. It is the final enzyme in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechol, converting the acetaldehyde produced by EC 4.1.3.39 into acetyl-CoA [3]. NADP+ can replace NAD+ but the rate of reaction is much slower [3]. |
| Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, METACYC, CAS registry number: 9028-91-5 |
| References: |
| 1. |
Burton, R.M. and Stadtman, E.R. The oxidation of acetaldehyde to acetyl coenzyme A. J. Biol. Chem. 202 (1953) 873–890. [PMID: 13061511] |
| 2. |
Smith, L.T. and Kaplan, N.O. Purification, properties, and kinetic mechanism of coenzyme A-linked aldehyde dehydrogenase from Clostridium kluyveri. Arch. Biochem. Biophys. 203 (1980) 663–675. [PMID: 7458347] |
| 3. |
Powlowski, J., Sahlman, L. and Shingler, V. Purification and properties of the physically associated meta-cleavage
pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde
dehydrogenase (acylating) from Pseudomonas sp. strain CF600. J. Bacteriol. 175 (1993) 377–385. [PMID: 8419288] |
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| [EC 1.2.1.10 created 1961, modified 2006, modified 2011] |
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