Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain | |||||||||||
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Identifiers | |||||||||||
Symbol | Ald_Xan_dh_C | ||||||||||
Pfam | PF01315 | ||||||||||
InterPro | IPR000674 | ||||||||||
SCOP2 | 1alo / SCOPe / SUPFAM | ||||||||||
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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.
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||||
Symbol | Ald_Xan_dh_C | ||||||||||
Pfam | PF01315 | ||||||||||
InterPro | IPR000674 | ||||||||||
SCOP2 | 1alo / SCOPe / SUPFAM | ||||||||||
|
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.