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.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .

References

• Mackinnon CM, Carter PE, Smyth SJ, Dunbar B, Fothergill JE "Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence". Eur. J. Biochem. 169 547–53.
• SNOKE JE, YANARI S, BLOCH K "Synthesis of glutathione from gamma-glutamylcysteine". J. Biol. Chem. 201 573–86.
• MANDELES S, BLOCK K "Enzymatic synthesis of gamma-glutamylcysteine". J. Biol. Chem. 214 639–46.

External links

The CAS registry number for this enzyme class is .

Gene Ontology (GO) codes