Glutathione synthetase
| glutathione synthetase | |||||||
|---|---|---|---|---|---|---|---|
| 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 | ||||||
| |||||||
| Eukaryotic glutathione synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 human glutathione synthetase | |||||||||
| Identifiers | |||||||||
| Symbol | GSH_synthase | ||||||||
| Pfam | PF03199 | ||||||||
| Pfam clan | CL0483 | ||||||||
| InterPro | IPR004887 | ||||||||
| SCOP2 | 2hgs / SCOPe / SUPFAM | ||||||||
| |||||||||
| Eukaryotic glutathione synthase, ATP binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
human glutathione synthetase | |||||||||
| Identifiers | |||||||||
| Symbol | GSH_synth_ATP | ||||||||
| Pfam | PF03917 | ||||||||
| InterPro | IPR005615 | ||||||||
| SCOP2 | 1m0t / SCOPe / SUPFAM | ||||||||
| |||||||||
| 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 | ||||||||
| |||||||||
| 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 | ||||||||
| |||||||||
Glutathione synthetase (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione.[1]
In eukaryotes, this is a homodimeric enzyme. In humans, defects in GSS are inherited in an autosomal recessive way and are the cause of severe metabolic acidosis, 5-oxoprolinuria, and increased rate of haemolysis and defective function of the central nervous system. The substrate-binding domain has a 3-layer alpha/beta/alpha structure.[2]
See also
References
- ^ Njålsson R, Norgren S (2005). "Physiological and pathological aspects of GSH metabolism". Acta Paediatr. 94 (2): 132–7. doi:10.1080/08035250410025285. PMID 15981742.
- ^ Polekhina G, Board PG, Gali RR, Rossjohn J, Parker MW (1999). "Molecular basis of glutathione synthetase deficiency and a rare gene permutation event". EMBO J. 18 (12): 3204–13. doi:10.1093/emboj/18.12.3204. PMC 1171401. PMID 10369661.
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External links
- Glutathione+Synthetase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)