Glutathione synthase

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	OMIM : 601002 ; UniProt : P48637 ;
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

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 .

[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 .