| Description | A number of different eukaryotic oxidoreductases that require and bind a molybdopterin cofactor have been shown [ ] to share a few regions of sequence similarity. These enzymes include xanthine dehydrogenase (), aldehyde oxidase ( ), nitrate reductase ( ), and sulphite oxidase ( ). The multidomain redox enzyme NAD(P)H:nitrate reductase (NR) catalyses the reduction of nitrate to nitrite in a single polypeptide electron transport chain with electron flow from NAD(P)H-FAD-cytochrome b5-molybdopterin-NO(3). Three forms of NR are known, an NADH-specific enzyme found in higher plants and algae ( ); an NAD(P)H-bispecific enzyme found in higher plants, algae and fungi ( ); and an NADPH-specific enzyme found only in fungi ( ) [ ]. The mitochondrial enzyme sulphite oxidase (sulphite:ferricytochrome c oxidoreductase; ) catalyses oxidation of sulphite to sulphate, using cytochrome c as the physiological electron acceptor. Sulphite oxidase consists of two structure/function domains, an N-terminal haem domain, similar to cytochrome b5; and a C-terminal molybdopterin domain [ ].Despite functional parallels, members of the family show no sequence similarity to the C-terminal molybdopterin domain of xanthine dehydrogenase, although xanthine dehydrogenase, nitrate reductases and sulphite oxidase all contain the eukaryotic molybdopterin oxidoreductases signature. Sequence comparison suggests that only a single Cys residue (Cys186 in chicken sulphite oxidase), is invariant in all these enzymes, indicating that it may play a role in binding molybdopterin to the protein [ , ]. | Name | Eukaryotic molybdopterin oxidoreductase |
| Short Name | Mopterin_OxRdtase_euk | Type | Family |
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