Biology:Aldehyde dehydrogenase (FAD-independent)
From HandWiki
Short description: Enzyme in the family of oxidoreductases
| Aldehyde dehydrogenase (FAD-independent) | |||||||||
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| Identifiers | |||||||||
| EC number | 1.2.99.7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, an aldehyde dehydrogenase (FAD-independent) (EC 1.2.99.7) is an enzyme that catalyzes the chemical reaction
- an aldehyde + H2O + acceptor [math]\displaystyle{ \rightleftharpoons }[/math] a carboxylate + reduced acceptor
The 3 substrates of this enzyme are aldehyde, H2O, and acceptor, whereas its two products are carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:acceptor oxidoreductase (FAD-independent). Other names in common use include aldehyde oxidase, aldehyde oxidoreductase, Mop, and AORDd.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1ZCS.
References
- "Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690". FEMS Microbiol. Lett. 229 (1): 31–6. 2003. doi:10.1016/S0378-1097(03)00781-X. PMID 14659539.
- MJ, Moura JJ; Archer, M; Dias, JM; Bursakov, S; Huber, R; Moura, I; Romão, MJ; Moura, JJ (2000). "Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from Desulfovibrio desulfuricans ATCC 27774". Biochem. Biophys. Res. Commun. 268 (3): 745–9. doi:10.1006/bbrc.2000.2135. PMID 10679276.
- "Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491 EPR assignment of the proximal [2Fe-2S] cluster to the Mo site". Eur. J. Biochem. 267 (7): 2054–61. 2000. doi:10.1046/j.1432-1327.2000.01209.x. PMID 10727945.
- "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas". Science 270 (5239): 1170–6. 1995. doi:10.1126/science.270.5239.1170. PMID 7502041. Bibcode: 1995Sci...270.1170R.
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