| 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 |
| SCOP |
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]
[edit] See also
[edit] 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 (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171401.
[edit] External links
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| 6.1: Carbon-Oxygen |
Aminoacyl tRNA synthetase ( Tyrosine, Tryptophan, Threonine, Leucine, Isoleucine, Lysine, Alanine, Valine, Methionine, Serine, Aspartate, D-alanine-poly(phosphoribitol) ligase, Glycine, Proline, Cysteine, Glutamate, Glutamine, Arginine, Phenylalanine, Histidine, Asparagine, Aspartate, Glutamate, Lysine)
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| 6.2: Carbon-Sulfur |
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| 6.3: Carbon-Nitrogen |
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| 6.5: Phosphoric Ester |
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| 6.6: Nitrogen-Metal |
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