Aldehyde dehydrogenase (FAD-independent)

Aldehyde dehydrogenase (FAD-independent)
Identifiers
EC no.	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
Search PMC articles PubMed articles NCBI proteins

In enzymology, an aldehyde dehydrogenase (FAD-independent) (EC 1.2.99.7) is an enzyme that catalyzes the chemical reaction

an aldehyde + H₂O + acceptor ${\displaystyle \rightleftharpoons }$ 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

• Fujishiro K, Aisaka K, Uwajima T (2003). "Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690". FEMS Microbiol. Lett. 229 (1): 31–6. 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.
• Andrade SL, Brondino CD, Feio MJ, Moura I, Moura JJ (2000). "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. doi:10.1046/j.1432-1327.2000.01209.x. PMID 10727945.
• Romão MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider M, Hof P, Huber R (1995). "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas". Science. 270 (5239): 1170–6. Bibcode:1995Sci...270.1170R. doi:10.1126/science.270.5239.1170. PMID 7502041. S2CID 34922450.