Aldehyde dehydrogenase (FAD-independent)

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 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.

v t e Aldehyde/oxo oxidoreductases (EC 1.2)
1.2.1: NAD or NADP	Aldehyde dehydrogenase Acetaldehyde dehydrogenase Long-chain-aldehyde dehydrogenase Mycothiol-dependent formaldehyde dehydrogenase
1.2.2: cytochrome	Formate dehydrogenase (cytochrome)
1.2.3: oxygen	Aldehyde oxidase
1.2.4: disulfide	Oxoglutarate dehydrogenase complex Pyruvate dehydrogenase Branched-chain alpha-keto acid dehydrogenase complex BCKDHA BCKDHB DBT DLD
1.2.7: iron–sulfur protein	Pyruvate synthase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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