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2.8.1.9 |
Description |
Molybdenum cofactor sulfurtransferase |
Alternative names |
molybdenum cofactor sulfurase; ABA3; HMCS; MoCo sulfurase; MoCo sulfurtransferase; L-cysteine:molybdenum cofactor sulfurtransferase.
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Catalyzed reaction |
molybdenum cofactor + L-cysteine + 2 H+ = thio-molybdenum cofactor + L-alanine + H2O |
Cofactor |
Pyridoxal-phosphate. |
Comments |
Contains pyridoxal phosphate. Replaces the equatorial oxo ligand of the molybdenum by sulfur via an enzyme-bound persulfide. The reaction occurs in prokaryotes and eukaryotes but MoCo sulfurtransferases are only found in eukaryotes. In prokaryotes the reaction is catalysed by two enzymes: cysteine desulfurase (EC 2.8.1.7), which is homologous to the N-terminus of eukaryotic MoCo sulfurtransferases, and a molybdo-enzyme specific chaperone which binds the MoCo and acts as an adapter protein. |
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These desulfurases are eukariotic multidomain enzymes involved in the sulfuration of molybdenum enzyzmes such as xanthine oxidase.
Additional_domain JC7680 1-500 |
Diseases |
Xanthinuria types I and II |
Organisms |
-Plants -Metazoa -Human |
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Family |
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Links |
Enzyme (activities) 2.8.1.9
BRENDA (activities) 2.8.1.9
KEGG (pathways) 2.8.1.9
PLPMDB (PLP mutants) 2.8.1.9
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References |
Articles on 2.8.1.9 |
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last changed |
2017/09/14 09:49 |
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