Glutathione synthase
Glutathione synthase | ||
---|---|---|
Properties of human protein | ||
Mass / length primary structure | 474 amino acids | |
Secondary to quaternary structure | Homodimer | |
Cofactor | magnesium | |
Identifier | ||
Gene name | GSS | |
External IDs | ||
Enzyme classification | ||
EC, category | 6.3.2.3 , ligase | |
Response type | Peptide bond | |
Substrate | γ-glutamylcysteine, glycine, ATP | |
Products | Glutathione, ADP, phosphate | |
Occurrence | ||
Homology family | GS | |
Parent taxon | Creature | |
Orthologue | ||
human | House mouse | |
Entrez | 2937 | 14854 |
Ensemble | ENSG00000100983 | ENSMUSG00000027610 |
UniProt | P48637 | P51855 |
Refseq (mRNA) | NM_000178 | NM_008180 |
Refseq (protein) | NP_000169 | NP_032206 |
Gene locus | Chr 1: 34.93 - 34.96 Mb | Chr 2: 155.56 - 155.59 Mb |
PubMed search | 2937 |
14854
|
The glutathione synthetase (GSH-S) is the enzyme of glutathione - metabolism which the second step of glutathione synthesis catalyzed . Glutathione synthetase in most eukaryotes and bacteria in the cytosol localized, and is found in plants in the cytosol and plastids . When people can mutations in GSS - gene lead to a deficiency in the enzyme, the light and heavy progressive forms has ( hemolytic anemia ).
biochemistry
Glutathione synthase catalyzes the formation of a peptide bond between the carboxy group of a γ-glutamylcysteine molecule and the amino group of a glycine molecule , whereby glutathione is formed. The reaction is coupled with the cleavage of a molecule of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and phosphate .
The enzyme is inhibited by its products (negative feedback ).
structure
The glutathione synthetase is active as a homodimer. On the basis of sequence comparisons, two types can be distinguished, which occur in eukaryotes or in cyanobacteria , alpha and gamma proteobacteria .
In streptococci about a gene occurs also, which codes for a protein having the activity of glutathione synthetase and Glutamatcysteinligase united, thus capable of catalyzing the entire synthesis of glutathione from the amino acids.
swell
- Entry at BRENDA
- G. Noctor, L. Gomez, H. Vanacker, CH Foyer: Interactions between biosynthesis, compartmentation and transport in the control of glutathione homeostasis and signaling. In: J Exp Bot. Volume 53, 2002, pp. 1283-1304.
Individual evidence
- ↑ A. Wachter, S. Wolf, H. Steininger, J. Bogs, T. Rausch: Differential targeting of GSH1 and GSH2 is achieved by multiple transcription initiation: implications for the compartmentation of glutathione biosynthesis in the Brassicaceae. In: Plant J . No. 41 , 2005, p. 15-30 .
- ↑ SD Copley, JK Dhillon: Lateral gene transfer and parallel evolution in the history of glutathione biosynthesis genes. In: Genome Biol . No. 3 , 2002, research0025 .
- ↑ OW Griffith, BE Janowiak: Glutathione Synthesis in Streptococcus agalactiae: One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities . In: J. Biol. Chem. No. 12 , 2005, p. 11829-11839 .