Homoglutathione synthase | |||||||||
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Identifiers | |||||||||
EC no. | 6.3.2.23 | ||||||||
CAS no. | 113875-72-2 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a homoglutathione synthase (EC 6.3.2.23) is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are ATP, gamma-L-glutamyl-L-cysteine, and beta-alanine, whereas its 3 products are ADP, phosphate, and gamma-L-glutamyl-L-cysteinyl-beta-alanine.
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 gamma-L-glutamyl-L-cysteine:beta-alanine ligase (ADP-forming). Other names in common use include homoglutathione synthetase, and beta-alanine specific hGSH synthetase.
Glutathione synthetase (GSS) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione. Glutathione synthetase is also a potent antioxidant. It is found in many species including bacteria, yeast, mammals, and plants.
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