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+ \rightleftharpoons thio-molybdenum cofactor + L-alanine + H2O

This enzyme contains pyridoxal phosphate.

References

  1. Bittner, F., Oreb, M. and 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.
  2. Heidenreich, T., Wollers, S., Mendel, R.R. and 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.
  3. Wollers, S., Heidenreich, T., Zarepour, M., Zachmann, D., Kraft, C., Zhao, Y., Mendel, R.R. and 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

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