Function and Biology Details
Reactions catalysed:
A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
A glutathione-S-conjugate + H(2)O = an (L-cysteinylglycine)-S-conjugate + L-glutamate
Leukotriene C(4) + H(2)O = leukotriene D(4) + L-glutamate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Glutathione hydrolase 1 heavy chain (preferred)
PDBe Complex ID:
PDB-CPX-148579 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutathione hydrolase 1 heavy chain
Molecule details ›
Chain: A
Length: 353 amino acids
Theoretical weight: 38.53 KDa
Source organism: Homo sapiens
Expression system: Pichia
UniProt:
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Serum Albumin; Chain A, Domain 1
Length: 353 amino acids
Theoretical weight: 38.53 KDa
Source organism: Homo sapiens
Expression system: Pichia
UniProt:
- Canonical:
P19440 (Residues: 28-380; Coverage: 62%)
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Serum Albumin; Chain A, Domain 1
Glutathione hydrolase 1 light chain
Molecule details ›
Chain: B
Length: 189 amino acids
Theoretical weight: 20.01 KDa
Source organism: Homo sapiens
Expression system: Pichia
UniProt:
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Length: 189 amino acids
Theoretical weight: 20.01 KDa
Source organism: Homo sapiens
Expression system: Pichia
UniProt:
- Canonical: P19440 (Residues: 381-569; Coverage: 33%)
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
