Nonlinear Free Energy Relationship in the General-Acid-Catalyzed Acylation of Rat Kidney γ-Glutamyl Transpeptidase by a Series of γ-Glutamyl Anilide Substrate Analogues

The γ-glutamyl transpeptidase (GGT) purified from rat kidney reacts with a series of eight parasubstituted L-glutamyl γ-anilides, in the presence of Gly−Gly, catalyzing the formation of γ-Glu−Gly−Gly (pH 8.0, 37 °C). The transpeptidation reaction was followed through the discontinuous colorimetric d...

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Bibliographic Details
Published in:	Biochemistry (Easton) Vol. 40; no. 42; pp. 12678 - 12685
Main Authors:	Ménard, Annie, Castonguay, Roselyne, Lherbet, Christian, Rivard, Caroline, Roupioz, Yoann, Keillor, Jeffrey W
Format:	Journal Article
Language:	English
Published:	United States American Chemical Society 23-10-2001
Subjects:	Acylation Animals Binding Sites Catalysis Deuterium - chemistry Deuterium - metabolism Deuterium Oxide - chemistry Deuterium Oxide - metabolism Energy Metabolism gamma-Glutamyltransferase - chemistry gamma-Glutamyltransferase - metabolism Glutamine - analogs & derivatives Glutamine - chemical synthesis Glutamine - metabolism Hydrogen-Ion Concentration Kidney - enzymology Kinetics Male Protons Rats Rats, Sprague-Dawley Substrate Specificity Temperature
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