Glutathione synthetase
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| glutathione synthetase | |
|---|---|
| Identifiers | |
| Symbol | GSS |
| Entrez | 2937 |
| HUGO | 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 |
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| Identifiers | |||||||||
| Symbol | GSH_synthase | ||||||||
| Pfam | PF03199 | ||||||||
| Pfam clan | CL0483 | ||||||||
| InterPro | IPR004887 | ||||||||
| SCOP | 2hgs | ||||||||
| SUPERFAMILY | 2hgs | ||||||||
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| Eukaryotic glutathione synthase, ATP binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
human glutathione synthetase |
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| Identifiers | |||||||||
| Symbol | GSH_synth_ATP | ||||||||
| Pfam | PF03917 | ||||||||
| InterPro | IPR005615 | ||||||||
| SCOP | 1m0t | ||||||||
| SUPERFAMILY | 1m0t | ||||||||
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| Prokaryotic glutathione synthetase, N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 structure of escherichia coli glutathione synthetase at ph 7.5 |
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| Identifiers | |||||||||
| Symbol | GSH-S_N | ||||||||
| Pfam | PF02951 | ||||||||
| InterPro | IPR004215 | ||||||||
| SCOP | 1glv | ||||||||
| SUPERFAMILY | 1glv | ||||||||
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| Prokaryotic glutathione synthetase, ATP-grasp domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
structure of escherichia coli glutathione synthetase at ph 7.5 |
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| Identifiers | |||||||||
| Symbol | GSH-S_ATP | ||||||||
| Pfam | PF02955 | ||||||||
| Pfam clan | CL0179 | ||||||||
| InterPro | IPR004218 | ||||||||
| SCOP | 1glv | ||||||||
| SUPERFAMILY | 1glv | ||||||||
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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[edit]
References[edit]
- ^ 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 (June 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.
External links[edit]
- Glutathione Synthetase at the US National Library of Medicine Medical Subject Headings (MeSH)
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