Glutamate-cysteine ligase

From Wikipedia, the free encyclopedia

In enzymology, a glutamate-cysteine ligase (EC 6.3.2.2) is an enzyme that catalyzes the chemical reaction

ATP + L-glutamate + L-cysteine $\rightleftharpoons$ ADP + phosphate + gamma-L-glutamyl-L-cysteine

The 3 substrates of this enzyme are ATP, L-glutamate, and L-cysteine, whereas its 3 products are ADP, phosphate, and gamma-L-glutamyl-L-cysteine.

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is L-glutamate:L-cysteine gamma-ligase (ADP-forming). Other names in common use include gamma-glutamylcysteine synthetase, gamma-glutamyl-L-cysteine synthetase, and gamma-glutamylcysteinyl synthetase. This enzyme participates in glutamate metabolism and glutathione metabolism. At least one compound, [[S-Butyl-DL-homocysteine-[S,R]-sulfoximine]] is known to inhibit this enzyme.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1V4G, 1VA6, 2D32, 2D33, 2GWC, and 2GWD.

[edit] References

IUBMB entry for 6.3.2.2
BRENDA references for 6.3.2.2 (Recommended.)
PubMed references for 6.3.2.2
PubMed Central references for 6.3.2.2
Google Scholar references for 6.3.2.2
Mackinnon CM, Carter PE, Smyth SJ, Dunbar B, Fothergill JE (1987). "Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence". Eur. J. Biochem. 169: 547–53. doi:10.1111/j.1432-1033.1987.tb13644.x. PMID 3500856.
SNOKE JE, YANARI S, BLOCH K (1953). "Synthesis of glutathione from gamma-glutamylcysteine". J. Biol. Chem. 201: 573–86. PMID 13061393.
MANDELES S, BLOCK K (1955). "Enzymatic synthesis of gamma-glutamylcysteine". J. Biol. Chem. 214: 639–46. PMID 14381401.