CHAC1,2 cleaves GSH to OPRO and CysGly

Stable Identifier
R-HSA-6785928
Type
Reaction
Species
Homo sapiens
Compartment
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Glutathione-specific gamma-glutamylcyclotransferases 1 and 2 (CHAC1 and 2) catalyse the specific cleavage of glutathione (GSH) into 5-oxoproline (OPRO) and a cysteinylglycine (CysGly) dipeptide. GSH acts a redox buffer in cells and its depletion is an important factor for apoptosis, oxidative stress and progression of cancer. CHAC1 and 2 act as proapototic agents with implications for human health and disease (Mungrue et al. 2009, Crawford et al. 2015).

Literature References
PubMed ID Title Journal Year
25931127 Human CHAC1 Protein Degrades Glutathione, and mRNA Induction Is Regulated by the Transcription Factors ATF4 and ATF3 and a Bipartite ATF/CRE Regulatory Element

Crawford, RR, Prescott, ET, Sylvester, CF, Higdon, AN, Shan, J, Kilberg, MS, Mungrue, IN

J. Biol. Chem. 2015
19109178 CHAC1/MGC4504 is a novel proapoptotic component of the unfolded protein response, downstream of the ATF4-ATF3-CHOP cascade

Mungrue, IN, Pagnon, J, Kohannim, O, Gargalovic, PS, Lusis, AJ

J. Immunol. 2009
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
gamma-glutamylcyclotransferase activity of CHAC1,2 [cytosol]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed
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