Glutathione synthase

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Glutathione synthase

Existing structural data : 2hgs

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

  1. 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 .
  2. SD Copley, JK Dhillon: Lateral gene transfer and parallel evolution in the history of glutathione biosynthesis genes. In: Genome Biol . No. 3 , 2002, research0025 .
  3. 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 .