Structure of escherichia coli glutathione synthetase at ph 7.5
Identifiers
Symbol
GSH-S_ATP
Pfam
PF02955
Pfam clan
CL0179
InterPro
IPR004218
SCOP2
1glv / SCOPe / SUPFAM
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Glutathione synthetase (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione.[2] Glutathione synthetase is also a potent antioxidant. It is found in many species including bacteria, yeast, mammals, and plants.[3]
In humans, defects in GSS are inherited in an autosomal recessive way and are the cause of severe metabolic acidosis, 5-oxoprolinuria, increased rate of haemolysis, and defective function of the central nervous system.[4] Deficiencies in GSS can cause a spectrum of deleterious symptoms in plants and human beings alike.[5]
In eukaryotes, this is a homodimeric enzyme. The substrate-binding domain has a three-layer alpha/beta/alpha structure.[6] This enzyme utilizes and stabilizes an acylphosphate intermediate to later perform a favorable nucleophilic attack of glycine.
^Gogos A, Shapiro L (Dec 2002). "Large conformational changes in the catalytic cycle of glutathione synthase". Structure. 10 (12): 1669–76. doi:10.1016/S0969-2126(02)00906-1. PMID 12467574.
^Njålsson R, Norgren S (2005). "Physiological and pathological aspects of GSH metabolism". Acta Paediatr. 94 (2): 132–7. doi:10.1080/08035250410025285. PMID 15981742.
^Li H, Xu H, Graham DE, White RH (Aug 2003). "Glutathione synthetase homologs encode alpha-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses". Proceedings of the National Academy of Sciences of the United States of America. 100 (17): 9785–90. Bibcode:2003PNAS..100.9785L. doi:10.1073/pnas.1733391100. PMC 187843. PMID 12909715.
^Cite error: The named reference Njålsson_2005 was invoked but never defined (see the help page).
^O'Neill M. "Glutathione Synthetase Deficiency". Online Mendelian Inheritance in Man.
^Cite error: The named reference Polekhina_1999 was invoked but never defined (see the help page).
and 24 Related for: Glutathione synthetase information
Glutathionesynthetase (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine...
in glutathione synthesis. Second, glycine is added to the C-terminal of γ-glutamylcysteine. This condensation is catalyzed by glutathionesynthetase. While...
Glutathionesynthetase deficiency (GSD) is a rare autosomal recessive metabolic disorder that prevents the production of glutathione. Glutathione helps...
the enzymes glutamate–cysteine ligase (GCL) and glutathionesynthetase (GSS) to produce glutathione. Harris Ripps, Wen Shen (2012). "Review: Taurine:...
ligase (forms an isopeptide bond, which is not a peptide bond) and glutathionesynthetase (forms a peptide bond). A peptide bond can be broken by hydrolysis...
Genetic significant dose German shepherd dog Global Species Database Glutathionesynthetase deficiency Glycogen storage disease GSD microscopy GSD chemical...
believed mechanism for synthetase activity is that first glutathione and Mg2+-ATP bind to the enzyme in a ternary complex where glutathione becomes activated...
cysteine. This dipeptide is then condensed with glycine by glutathionesynthetase to form glutathione. In chemistry, peptides are synthesized by a variety of...
serine) catalyzed by glutathionesynthetase. Both steps of the synthesis of glutathione are ATP dependent reactions. Glutathione is maintained in the...
corresponding alcohols. GPx1 typically uses glutathione (GSH) as the reductant, but when glutathionesynthetase (GSS) is, as in brain mitochondria, γ-glutamylcysteine...
element-binding protein 2 GNAS1: Gs alpha subunit (membrane G-protein) GSS: glutathionesynthetase HSPA12B: encoding protein Heat shock protein family a (hsp70) member...
The compound inhibits gamma-glutamylcysteine synthetase, the enzyme required in the first step of glutathione synthesis. Buthionine sulfoximine may also...
same enzymes that create GSH, namely Glutamate–cysteine ligase and glutathionesynthetase. Major regulators of OPH biosynthesis are local (relative) concentrations...
anemia due to gamma-glutamylcysteine synthetase deficiency; 230450; GCLC Hemolytic anemia due to glutathionesynthetase deficiency; 231900; GSS Hemolytic...
ligase, also known as gamma-glutamylcysteine synthetase, is the first rate limiting enzyme of glutathione synthesis. The enzyme consists of two subunits...
synthase (EC 6.3.1.8) is an enzyme that catalyzes the chemical reaction glutathione + spermidine + ATP ⇌ {\displaystyle \rightleftharpoons } glutathionylspermidine...
the sulfur. Selenocysteine is present in several enzymes (for example glutathione peroxidases, tetraiodothyronine 5′ deiodinases, thioredoxin reductases...
8-tetrahydrosarcinapterin. Li H, Xu H, Graham DE, White RH (August 2003). "Glutathionesynthetase homologs encode alpha-L-glutamate ligases for methanogenic coenzyme...
encoded by sodA and sodB), catalases (katE and katG), glutathionesynthetase (gshAB) and glutathione reductase (gor). Some bacteria have NADH-dependent peroxidases...
homoglutathione synthetase, and beta-alanine specific hGSH synthetase. Macnicol PK (1987). "Homoglutathione and glutathionesynthetases of legume seedlings...
\rightleftharpoons } glutathione + spermidine Thus, the two substrates of this enzyme are glutathionylspermidine and H2O, whereas its two products are glutathione and...
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