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Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain

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Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain
Identifiers
SymbolAld_Xan_dh_C
PfamPF01315
InterProIPR000674
SCOP21alo / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1t3qE: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

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Further reading

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  • 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