Biology:Molybdenum cofactor sulfurtransferase
From HandWiki
| 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 | ||||||||
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Molybdenum cofactor sulfurtransferase (EC 2.8.1.9, molybdenum cofactor sulfurase, ABA3, 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+ [math]\displaystyle{ \rightleftharpoons }[/math] thio-molybdenum cofactor + L-alanine + H2O
This enzyme contains pyridoxal phosphate.
References
- ↑ "ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana". The Journal of Biological Chemistry 276 (44): 40381–4. November 2001. doi:10.1074/jbc.c100472200. PMID 11553608.
- ↑ "Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration". The Journal of Biological Chemistry 280 (6): 4213–8. February 2005. doi:10.1074/jbc.m411195200. PMID 15561708.
- ↑ "Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration". The Journal of Biological Chemistry 283 (15): 9642–50. April 2008. 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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