Evidence for an arginine residue at the coenzyme-binding site of Escherichia coli isocitrate dehydrogenase

McKee, J.S. and Nimmo, H.G. (1989) Evidence for an arginine residue at the coenzyme-binding site of Escherichia coli isocitrate dehydrogenase. Biochemical Journal, 261(1), pp. 301-304. (doi:10.1042/bj2610301) (PMID:2673216) (PMCID:PMC1138819)

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Abstract

The arginine-specific reagent phenylglyoxal inactivated the active, dephosphorylated, form of Escherichia coli isocitrate dehydrogenase rapidly in a pseudo-first-order process. Both NADP+ and NADPH protected the enzyme against inactivation. Phenylglyoxal appeared to react with one arginine residue per subunit, and the extent of the reaction was proportional to the extent of the inactivation. In contrast, the phosphorylated form of isocitrate dehydrogenase did not react detectably with phenylglyoxal. The data indicate that the coenzyme-binding site of isocitrate dehydrogenase contains a reactive arginine residue that is protected by phosphorylation, and are consistent with the hypothesis that phosphorylation of the enzyme occurs close to or at its active site.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Nimmo, Professor Hugh
Authors: McKee, J.S., and Nimmo, H.G.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Biochemical Journal
Publisher:Portland Press
ISSN:0264-6021
ISSN (Online):1470-8728

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