| EC |
1.2.1.30 |
| Accepted name: |
carboxylate reductase (NADP+) |
| Reaction: |
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP |
| Other name(s): |
aromatic acid reductase; aryl-aldehyde dehydrogenase (NADP+) |
| Systematic name: |
aryl-aldehyde:NADP+ oxidoreductase (ATP-forming) |
| Comments: |
The enzyme contains an adenylation domain, a phosphopantetheinyl binding domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the phosphopantetheinyl binding domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to an aldehyde and released. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9074-94-6 |
| References: |
| 1. |
Gross, G.G. and Zenk, M.H. Reduktion aromatischer Säuer zu Aldehyden und Alkoholen im zellfreien System. 1. Reinigung und Eigenschaften von Aryl-Aldehyd:NADP-Oxidoreduktase aus Neurospora crassa. Eur. J. Biochem. 8 (1969) 413–419. [DOI] [PMID: 4389863] |
| 2. |
Gross, G.G. Formation and reduction of intermediate acyladenylate by aryl-aldehyde. NADP oxidoreductase from Neurospora crassa. Eur. J. Biochem. 31 (1972) 585–592. [DOI] [PMID: 4405494] |
| 3. |
Venkitasubramanian, P., Daniels, L. and Rosazza, J.P. Reduction of carboxylic acids by Nocardia aldehyde oxidoreductase requires a phosphopantetheinylated enzyme. J. Biol. Chem. 282 (2007) 478–485. [PMID: 17102130] |
| 4. |
Stolterfoht, H., Schwendenwein, D., Sensen, C.W., Rudroff, F. and Winkler, M. Four distinct types of E.C. 1.2.1.30 enzymes can catalyze the reduction of carboxylic acids to aldehydes. J. Biotechnol. 257 (2017) 222–232. [PMID: 28223183] |
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| [EC 1.2.1.30 created 1972, modified 2019] |
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