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• W2022475786 abstract "γ-Glutamyl transpeptidase, from sprouting onion bulbs, was purified to homogeneity and characterized as a glycoprotein of Mr, 56 700. Studies to determine the mode of action of purified enzyme were carried out using the synthetic substrate γ-glutamyl p-nitroanilide. At pH 6.0, equal amounts of two products, glutamic acid and p- nitroaniline, were formed, demonstrating hydrolysis of the γ-glutamyl substrate. Between pH 6.0 and 9.0, the ratio of p- nitroaniline to glutamic acid increased from 1:1 to 17:1 indicating autotranspeptidation of γ-glutamyl p-nitroanilide. The enzyme showed a wide range of substrate specificity for intermediates in the biosynthetic pathway to flavour precursors. γ-Glutamyl transpeptidase was detected in leaves, roots and bulbs of the growing plant, but not in dormant bulbs. In vivo the enzyme acts as a hydrolase of γ-glutamyl peptides during the biosynthesis of flavour precursors." @default.
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• W2022475786 date "1994-08-01" @default.
• W2022475786 modified "2023-09-26" @default.
• W2022475786 title "Characterization of purified γ-glutamyl transpeptidase in onions: Evidence for in vivo role as a peptidase" @default.
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• W2022475786 doi "https://doi.org/10.1016/s0031-9422(00)89723-x" @default.
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