SSF54665

CO dehydrogenase molybdoprotein N-domain-like

SUPERFAMILY entry
Member databaseSUPERFAMILY
SUPERFAMILY typehomologous superfamily

Description
Imported from IPR036856

Aldehyde oxidase (
1.2.3.1
) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase (
1.1.1.204
) catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase (
1.1.3.22
) activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.

The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain
[1, 2]
. The core structure of this domain has a β-β-α-β-β-β-α fold and contains a β-hammerhead motif similar to that in barrel-sandwich hybrids.

References
Imported from IPR036856

1.Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. Romao MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider M, Hof P, Huber R. Science 270, 1170-6, (1995). View articlePMID: 7502041

2.Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. Dobbek H, Gremer L, Meyer O, Huber R. Proc. Natl. Acad. Sci. U.S.A. 96, 8884-9, (1999). View articlePMID: 10430865

Integrated to
External Links
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.