| Molybdenum cofactor sulfurtransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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, 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 RR (November 2001). "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. doi:10.1074/jbc.c100472200. PMID 11553608.
- ^ Heidenreich T, Wollers S, Mendel RR, Bittner F (February 2005). "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. doi:10.1074/jbc.m411195200. PMID 15561708.
- ^ Wollers S, Heidenreich T, Zarepour M, Zachmann D, Kraft C, Zhao Y, Mendel RR, Bittner F (April 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". The Journal of Biological Chemistry. 283 (15): 9642–50. doi:10.1074/jbc.m708549200. PMID 18258600.
External links
- Molybdenum+cofactor+sulfurtransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This page was last edited on 26 August 2023, at 14:59