Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain
| Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Ald_Xan_dh_C | ||||||||
| Pfam | PF01315 | ||||||||
| InterPro | IPR000674 | ||||||||
| SCOP | 1alo | ||||||||
| SUPERFAMILY | 1alo | ||||||||
| |||||||||
The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain.
Aldehyde oxidase (EC 1.2.3.1) catalyzes 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 (EC 1.1.1.204) catalyzes 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 (EC 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 sulfhydryl groups.
Human proteins containing this domain
Further reading
- Romão MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider M, Hof P, Huber R (November 1995). "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas". Science 270 (5239): 1170–6. doi:10.1126/science.270.5239.1170. PMID 7502041.
- Dobbek H, Gremer L, Meyer O, Huber R (August 1999). "Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine". Proc. Natl. Acad. Sci. U.S.A. 96 (16): 8884–9. doi:10.1073/pnas.96.16.8884. PMC 17702. PMID 10430865.
This article incorporates text from the public domain Pfam and InterPro IPR000674