Molybdenum cofactor sulfurtransferase
| Molybdenum cofactor sulfurtransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.8.1.9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Molybdenum cofactor sulfurtransferase (EC 2.8.1.9, molybdenum cofactor sulfurase, ABA3, HMCS, MoCo sulfurase, MoCo sulfurtransferase) is an enzyme with systematic name L-cysteine:molybdenum cofactor sulfurtransferase.[1][2][3] This enzyme catalyses the following chemical reaction
- molybdenum cofactor + L-cysteine + 2 H+ thio-molybdenum cofactor + L-alanine + H2O
This enzyme contains pyridoxal phosphate.
References
- ↑ Bittner, F.; Oreb, M.; Mendel, R.R. (2001). "ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana". J. Biol. Chem. 276: 40381–40384. doi:10.1074/jbc.c100472200. PMID 11553608.
- ↑ Heidenreich, T.; Wollers, S.; Mendel, R.R.; Bittner, F. (2005). "Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration". J. Biol. Chem. 280: 4213–4218. doi:10.1074/jbc.m411195200. PMID 15561708.
- ↑ Wollers, S.; Heidenreich, T.; Zarepour, M.; Zachmann, D.; Kraft, C.; Zhao, Y.; Mendel, R.R.; Bittner, F. (2008). "Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration". J. Biol. Chem. 283: 9642–9650. doi:10.1074/jbc.m708549200. PMID 18258600.
External links
- Molybdenum cofactor sulfurtransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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