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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 3.4.19.13

Accepted Name
Glutathione hydrolase.
Alternative Name(s)
Gamma-glutamyltranspeptidase.
Glutathionase.
Reaction catalysed
Glutathione + H(2)O <=> L-cysteinylglycine + L-glutamate
Comment(s)
  • This protein also has EC 2.3.2.2 activity.
  • The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide.
  • The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions.
  • The human enzyme also hydrolyzes oxidized glutathione and leukotriene C4 with similar efficiency, while the mouse enzyme does not.
Cross-references
BRENDA3.4.19.13
EC2PDB3.4.19.13
ExplorEnz3.4.19.13
PRIAM enzyme-specific profiles3.4.19.13
KEGG Ligand Database for Enzyme Nomenclature3.4.19.13
IUBMB Enzyme Nomenclature3.4.19.13
IntEnz3.4.19.13
MEDLINEFind literature relating to 3.4.19.13
MetaCyc3.4.19.13
UniProtKB/Swiss-Prot
Q05902, ECM38_YEAST;  Q8VYW6, GAGT1_ARATH;  Q680I5, GAGT2_ARATH;  
Q9M0G0, GAGT3_ARATH;  D4B387, GGT1_ARTBC;  P19440, GGT1_HUMAN;  
Q60928, GGT1_MOUSE;  P20735, GGT1_PIG;  P07314, GGT1_RAT;  
Q9US04, GGT1_SCHPO;  O14194, GGT2_SCHPO;  A6NGU5, GGT3_HUMAN;  
P36269, GGT5_HUMAN;  Q9Z2A9, GGT5_MOUSE;  Q9QWE9, GGT5_RAT;  
A7YWM1, GGT6_BOVIN;  Q6P531, GGT6_HUMAN;  Q6PDE7, GGT6_MOUSE;  
Q6IE08, GGT6_RAT;  Q0V8L2, GGT7_BOVIN;  Q9UJ14, GGT7_HUMAN;  
Q99JP7, GGT7_MOUSE;  Q99MZ4, GGT7_RAT;  P63186, GGT_BACNA;  
P54422, GGT_BACSU;  P18956, GGT_ECOLI;  Q9I406, GGT_PSEAE;  
P36267, GGT_PSEUA;  P74181, GGT_SYNY3;  P15557, PAC1_PSES3;  
Q05053, PAC1_PSESV;  B8NM71, USTH_ASPFN;  O05218, YWRD_BACSU;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.19.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-