NDLI: Probing the location and function of the conserved histidine residue of phosphoglucose isomerase by using an active site directed inhibitor N-bromoacetylethanolamine phosphate.

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Probing the location and function of the conserved histidine residue of phosphoglucose isomerase by using an active site directed inhibitor N-bromoacetylethanolamine phosphate.

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Probing the location and function of the conserved histidine residue of phosphoglucose isomerase by using an active site directed inhibitor N-bromoacetylethanolamine phosphate.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Meng, M. Chane, T. L. Hsiao, C. D. Sun, Y. J.
Description	Country affiliation: China Author Affiliation: Meng M ( Graduate Institute of Agricultural Biotechnology, National Chung Hsing University, Taichung, Taiwan, Republic of China. mhmeng@dragon.nchu.edu.tw)
Abstract	Phosphoglucose isomerase (EC 5.3.1.9) catalyzes the interconversion of D-glucopyranose-6-phosphate and D-fructofuranose-6-phosphate by promoting an intrahydrogen transfer between C1 and C2. A conserved histidine exists throughout all phosphoglucose isomerases and was hypothesized to be the base catalyzing the isomerization reaction. In the present study, this conserved histidine, His311, of the enzyme from Bacillus stearothermophilus was subjected to mutational analysis, and the mutational effect on the inactivation kinetics by N-bromoacetylethanolamine phosphate was investigated. The substitution of His311 with alanine, asparagine, or glutamine resulted in the decrease of activity, in k(cat)/K(M), by a factor of 10(3), indicating the importance of this residue. N-bromoacetylethanolamine phosphate inactivated irreversibly the activity of wild-type phosphoglucose isomerase; however, His311 --> Ala became resistant to this inhibitor, indicating that His311 is located in the active site and is responsible for the inactivation of the enzyme by this active site-directed inhibitor. The pKa of His311 was estimated to be 6.31 according to the pH dependence of the inactivation. The proximity of this value with the pKa value of 6.35, determined from the pH dependence of k(cat)/K(M), supports a role of His311 as a general base in the catalysis.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	11
Volume Number	8
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1999-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Enzyme Inhibitors Pharmacology Ethanolamines Geobacillus Stearothermophilus Enzymology Glucose-6-phosphate Isomerase Chemistry Metabolism Histidine Amino Acid Sequence Amino Acid Substitution Animals Arabidopsis Binding Sites Conserved Sequence Escherichia Coli Antagonists & Inhibitors Kinetics Mice Molecular Sequence Data Mutagenesis, Site-directed Recombinant Proteins Saccharomyces Cerevisiae Zymomonas Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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