Autocatalytic Processing of γ-Glutamyltranspeptidase*

By Hideyuki Suzuki, H. Kumagai. Journal of Biological Chemistry, 2002

114 citations recorded by the source corpus.

γ-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 γ-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 γ-glutamyltranspeptidase ofEscherichia coli K-12 has been analyzed by means ofin vitro studies using purified precursors. Here we show that the processing of a precursor of γ-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 (β) subunit), which is also the nucleophile for the enzymatic reaction.

Subfields: Biochemistry, Materials Chemistry

View Paper: https://www.semanticscholar.org/paper/e83b05a28aaae157b2c039827a81b4749dd53a9d

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In Materials Chemistry

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Citations in the corpus

• Human and mouse proteases: a comparative genomic approach (2003, background): “These threonine proteases catalyse the degradation of glutathione to glutamic acid and cysteinyl glycin”