Glutathione synthetase
| Glutathione synthetase | |||||||
|---|---|---|---|---|---|---|---|
Structure of glutathione synthetase in yeast. Generated from 1M0W. | |||||||
| Identifiers | |||||||
| Symbol | GSS | ||||||
| NCBI gene | 2937 | ||||||
| HGNC | 4624 | ||||||
| OMIM | 601002 | ||||||
| RefSeq | NM_000178 | ||||||
| UniProt | P48637 | ||||||
| Other data | |||||||
| EC number | 6.3.2.3 | ||||||
| Locus | Chr. 20 q11.2 | ||||||
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| Eukaryotic glutathione synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Human glutathione synthetase | |||||||||
| Identifiers | |||||||||
| Symbol | GSH_synthase | ||||||||
| Pfam | PF03199 | ||||||||
| Pfam clan | CL0483 | ||||||||
| InterPro | IPR004887 | ||||||||
| SCOP2 | 2hgs / SCOPe / SUPFAM | ||||||||
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| glutathione synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
glutathione synthetase dimer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 6.3.2.3 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
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| Eukaryotic glutathione synthase, ATP binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Human glutathione synthetase | |||||||||
| Identifiers | |||||||||
| Symbol | GSH_synth_ATP | ||||||||
| Pfam | PF03917 | ||||||||
| InterPro | IPR005615 | ||||||||
| SCOP2 | 1m0t / SCOPe / SUPFAM | ||||||||
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| Prokaryotic glutathione synthetase, N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Structure of escherichia coli glutathione synthetase at ph 7.5 | |||||||||
| Identifiers | |||||||||
| Symbol | GSH-S_N | ||||||||
| Pfam | PF02951 | ||||||||
| InterPro | IPR004215 | ||||||||
| SCOP2 | 1glv / SCOPe / SUPFAM | ||||||||
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| Prokaryotic glutathione synthetase, ATP-grasp domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Structure of escherichia coli glutathione synthetase at ph 7.5 | |||||||||
| Identifiers | |||||||||
| Symbol | GSH-S_ATP | ||||||||
| Pfam | PF02955 | ||||||||
| Pfam clan | CL0179 | ||||||||
| InterPro | IPR004218 | ||||||||
| SCOP2 | 1glv / SCOPe / SUPFAM | ||||||||
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Glutathione synthetase (GSS) (EC 6.3.2.3) 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.
In humans, defects in GSS are inherited in an autosomal recessive way and are the cause of severe metabolic acidosis, 5-oxoprolinuria, increased rate of haemolysis, and defective function of the central nervous system. Deficiencies in GSS can cause a spectrum of deleterious symptoms in plants and human beings alike.
In eukaryotes, this is a homodimeric enzyme. The substrate-binding domain has a three-layer alpha/beta/alpha structure. This enzyme utilizes and stabilizes an acylphosphate intermediate to later perform a favorable nucleophilic attack of glycine.