Jump to content

Molybdenum cofactor sulfurtransferase

From Wikipedia, the free encyclopedia
Molybdenum cofactor sulfurtransferase
Identifiers
EC no.2.8.1.9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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

[edit]
  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
[edit]