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
SCOP2	1alo / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB 1t3qE:28-142 1n5wE:35-144 1zxiB:35-144 1n60B:35-144 1n63E:35-144 1n62E:35-144 1n61E:35-144 1sb3D:25-131 1rm6A:25-131 1wygA:587-693 1v97B:587-693 1n5xA:587-693 1fo4B:587-693 1vdvB:587-693 1fiqC:587-693 1dgjA:203-308 1sijA:192-308 1vlbA:192-308

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

• AOX1, XDH

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. Bibcode:1995Sci...270.1170R. doi:10.1126/science.270.5239.1170. PMID 7502041. S2CID 34922450.
• 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. Bibcode:1999PNAS...96.8884D. doi:10.1073/pnas.96.16.8884. PMC 17702. PMID 10430865.

This article incorporates text from the public domain Pfam and InterPro: IPR000674