PMID:12207027

Citation	Suzuki, H and Kumagai, H (2002) Autocatalytic processing of gamma-glutamyltranspeptidase. J. Biol. Chem. 277:43536-43
Abstract	gamma-Glutamyltranspeptidase is the key enzyme in glutathione metabolism, and we previously presented evidence suggesting that it belongs to the N-terminal nucleophile hydrolase superfamily. Enzymatically active gamma-glutamyltranspeptidase, which consists of one large subunit and one small subunit, is generated from an inactive common precursor through post-translational proteolytic processing. The processing mechanism for gamma-glutamyltranspeptidase of Escherichia coli K-12 has been analyzed by means of in vitro studies using purified precursors. Here we show that the processing of a precursor of gamma-glutamyltranspeptidase is an intramolecular autocatalytic event and that the catalytic nucleophile for the processing reaction is the oxygen atom of the side chain of Thr-391 (N-terminal residue of the small (beta) subunit), which is also the nucleophile for the enzymatic reaction.
Links	PubMed Online version:10.1074/jbc.M207680200
Keywords	Catalysis; Escherichia coli/enzymology; Hydroxylamine/pharmacology; Kinetics; Mutagenesis; Protease Inhibitors/pharmacology; Recombinant Fusion Proteins/pharmacology; Recombinant Proteins/metabolism; gamma-Glutamyltransferase/genetics; gamma-Glutamyltransferase/metabolism
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