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词条 Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain
释义

  1. Human proteins containing this domain

  2. Further reading

{{Pfam_box
| Symbol = Ald_Xan_dh_C
| Name = Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain
| image =
| width =
| caption =
| Pfam= PF01315
| InterPro= IPR000674
| SMART=
| Prosite =
| SCOP = 1alo
| TCDB =
| OPM family=
| OPM protein=
| PDB={{PDB3|1t3q}}E:28-142 {{PDB3|1n5w}}E:35-144 {{PDB3|1zxi}}B:35-144{{PDB3|1n60}}B:35-144 {{PDB3|1n63}}E:35-144 {{PDB3|1n62}}E:35-144{{PDB3|1n61}}E:35-144 {{PDB3|1sb3}}D:25-131 {{PDB3|1rm6}}A:25-131{{PDB3|1wyg}}A:587-693 {{PDB3|1v97}}B:587-693 {{PDB3|1n5x}}A:587-693{{PDB3|1fo4}}B:587-693 {{PDB3|1vdv}}B:587-693 {{PDB3|1fiq}}C:587-693{{PDB3|1dgj}}A:203-308 {{PDB3|1sij}}A:192-308 {{PDB3|1vlb}}A:192-308
}}

The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain.

Aldehyde oxidase ({{EC number|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 number|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 number|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

{{refbegin}}
  • {{cite journal |vauthors=Romão MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider M, Hof P, Huber R | title = Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas | journal = Science | volume = 270 | issue = 5239 | pages = 1170–6 |date=November 1995 | pmid = 7502041 | doi = 10.1126/science.270.5239.1170| url = | issn = }}
  • {{cite journal |vauthors=Dobbek H, Gremer L, Meyer O, Huber R | title = Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 16 | pages = 8884–9 |date=August 1999 | pmid = 10430865 | pmc = 17702 | doi = 10.1073/pnas.96.16.8884| url = | issn = }}
{{refend}}{{InterPro content|IPR000674}}{{DEFAULTSORT:Aldehyde oxidase and xanthine dehydrogenase, a b hammerhead domain}}{{protein-stub}}

1 : Protein domains

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