Glutathione synthetase

Glutathione synthetase
Structure of glutathione synthetase in yeast. Generated from 1M0W.[1]
Identifiers
SymbolGSS
NCBI gene2937
HGNC4624
OMIM601002
RefSeqNM_000178
UniProtP48637
Other data
EC number6.3.2.3
LocusChr. 20 q11.2
Search for
StructuresSwiss-model
DomainsInterPro
Eukaryotic glutathione synthase
Human glutathione synthetase
Identifiers
SymbolGSH_synthase
PfamPF03199
Pfam clanCL0483
InterProIPR004887
SCOP22hgs / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
glutathione synthase
glutathione synthetase dimer, Human
Identifiers
EC no.6.3.2.3
CAS no.9023-62-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Eukaryotic glutathione synthase, ATP binding domain
Human glutathione synthetase
Identifiers
SymbolGSH_synth_ATP
PfamPF03917
InterProIPR005615
SCOP21m0t / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Prokaryotic glutathione synthetase, N-terminal domain
Structure of escherichia coli glutathione synthetase at ph 7.5
Identifiers
SymbolGSH-S_N
PfamPF02951
InterProIPR004215
SCOP21glv / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Prokaryotic glutathione synthetase, ATP-grasp domain
Structure of escherichia coli glutathione synthetase at ph 7.5
Identifiers
SymbolGSH-S_ATP
PfamPF02955
Pfam clanCL0179
InterProIPR004218
SCOP21glv / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure 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.[citation needed]

  1. ^ 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.
  2. ^ Njålsson R, Norgren S (2005). "Physiological and pathological aspects of GSH metabolism". Acta Paediatr. 94 (2): 132–7. doi:10.1111/j.1651-2227.2005.tb01878.x. PMID 15981742.
  3. ^ 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.
  4. ^ Cite error: The named reference Njålsson_2005 was invoked but never defined (see the help page).
  5. ^ O'Neill M. "Glutathione Synthetase Deficiency". Online Mendelian Inheritance in Man. Archived from the original on 2016-02-10. Retrieved 2016-03-02.
  6. ^ Cite error: The named reference Polekhina_1999 was invoked but never defined (see the help page).