Glutathione synthetase
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.
| 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 | |||||||||
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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 | |||||||||
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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 | |||||||||
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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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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.