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Kinetic and spectroscopic study of slow-binding inhibition processes in aldolase

✍ Scribed by C. Blonski; T. Gefflaut; J. Perie


Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
120 KB
Volume
11
Category
Article
ISSN
0894-3230

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✦ Synopsis


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 bdicarbonyl 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.


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