Glutathione synthase
| glutathione synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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glutathione synthetase dimer, Human | |||||||||
| Identifiers | |||||||||
| EC number | 6.3.2.3 | ||||||||
| CAS number | 9023-62-5 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a glutathione synthase (EC 6.3.2.3) is an enzyme that catalyzes the chemical reaction
- ATP + gamma-L-glutamyl-L-cysteine + glycine ADP + phosphate + glutathione
The 3 substrates of this enzyme are ATP, gamma-L-glutamyl-L-cysteine, and glycine, whereas its 3 products are ADP, phosphate, and glutathione.
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:glycine ligase (ADP-forming). Other names in common use include glutathione synthetase, and GSH synthetase. This enzyme participates in glutamate metabolism and glutathione metabolism. At least one compound, Phosphinate is known to inhibit this enzyme.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1GLV, 1GSA, 1GSH, 1M0T, 1M0W, 2GLT, and 2HGS.
References
- Law MY; Halliwell B (1986). "Purification and properties of glutathione synthetase from (Spinacia oleracea) leaves". Plant Sci. 43 (3): 185–191. doi:10.1016/0168-9452(86)90016-6.
- Macnicol PK (1987). "Homoglutathione and glutathione synthetases of legume seedlings - partial-purification and substrate-specificity". Plant Sci. 53 (3): 229–235. doi:10.1016/0168-9452(87)90159-2.