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Kinetic and spectroscopic study of slow‐binding inhibition processes in aldolase
Author(s) -
Blonski C.,
Gefflaut T.,
Perie J.
Publication year - 1998
Publication title -
journal of physical organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.325
H-Index - 66
eISSN - 1099-1395
pISSN - 0894-3230
DOI - 10.1002/(sici)1099-1395(1998110)11:11<793::aid-poc60>3.0.co;2-m
Subject(s) - chemistry , aldolase a , kinetic energy , computational chemistry , stereochemistry , enzyme , organic chemistry , physics , quantum mechanics
Compounds similar in structure to reactants, intermediates and products of the aldolase‐catalysed reaction were synthesized and their affinities for the enzyme determined. The best situations were found with β‐dicarbonyl phosphorylated compounds which are a good mimics of the incoming groups in the bond‐forming process; the corresponding binding is characterized by slow‐binding inhibition type, the inhibitors forming stabilized iminium ions and enamines with the enzyme; similar effects were obtained with an aromatic aldehyde, also capable of forming a stabilized iminium ion. The use of aldolase mutants allows one to characterize the lysyl group involved in the process and also to suggest a proton transfer mechanism for the iminium ion formation with the enzyme natural substrate. © 1998 John Wiley & Sons, Ltd.