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Your query returned 1 entry. Printable version
EC | 3.4.19.13 | ||||||||||||||||||
Accepted name: | glutathione γ-glutamate hydrolase | ||||||||||||||||||
Reaction: | (1) glutathione + H2O = L-cysteinylglycine + L-glutamate (2) a glutathione-S-conjugate + H2O = an (L-cysteinylglycine)-S-conjugate + L-glutamate |
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Other name(s): | glutathionase; γ-glutamyltranspeptidase (ambiguous); glutathione hydrolase; GGT (gene name); ECM38 (gene name) | ||||||||||||||||||
Comments: | This is a bifunctional protein that also has the activity of EC 2.3.2.2, γ-glutamyltransferase. The enzyme binds its substrate by forming an initial γ-glutamyl-enzyme intermediate, releasing the L-cysteinylglycine part of the molecule. The enzyme then reacts with either a water molecule or a different acceptor substrate (usually an L-amino acid or a dipeptide) to form L-glutamate or a product containing a new γ-glutamyl isopeptide bond, respectively. The enzyme acts on glutathione, glutathione-S-conjugates, and, at a lower level, on other substrates with an N-terminal L-γ-glutamyl residue. It plays a crucial part in the glutathione-mediated xenobiotic detoxification pathway. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB | ||||||||||||||||||
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