Selective inhibition of metabolic enzymes by enzymatically synthesized D-glucal-6-phosphate.
Yeast hexokinase (EC 2.7.1.1) catalyzes the phosphorylation of D-glucal and methyl alpha- and beta-D-glucopyranosides at 1-5% of the rates of phosphorylation of D-glucose and 2-deoxy-D-glucose. Maltose, cellobiose, D-galactal and tetrahydropyran-2-methanol are not substrates of hexokinase. Enzymatically synthesized D-glucal-6-phosphate inhibits rabbit muscle phosphoglucose isomerase competitively (KI = 1.94 mM) and phosphoglucomutase noncompetitively (KI = 0.122 mM).
Chenault
H K
HK
Department of Chemistry and Biochemistry, University of Delaware, Newark 19716.
Mandes
R F
RF
D000818:Animals; D001667:Binding, Competitive; D002236:Carbohydrate Conformation; D005956:Glucose-6-Phosphate Isomerase / Q000037:antagonists & inhibitors*; D006593:Hexokinase / Q000378:metabolism*; D007700:Kinetics; D015394:Molecular Structure; D009132:Muscles / Q000201:enzymology; D010733:Phosphoglucomutase / Q000037:antagonists & inhibitors*; D011817:Rabbits; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013379:Substrate Specificity; D013403:Sugar Phosphates / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*
D013403:Sugar Phosphates; C092084:glucal-6-phosphate; D006593:Hexokinase; D005956:Glucose-6-Phosphate Isomerase; D010733:Phosphoglucomutase