Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.1.1 (hexokinase)
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Hexokinase from pyloric caeca of the starfish, Asterias amurensis, was purified to a specific activity of 148 units/mg protein. The purified enzyme appeared to be homogeneous on SDS-polyacrylamide gel electrophoresis. The molecular weight determined by SDS polyacrylamide gel electrophoresis and Ultrogel AcA 34 gel filtration was about 50,000. The enzyme showed a broad pH optimum ranging from 7.4 to 9.5. The Km values for D-glucose, D-fructose, 2-deoxy-D-glucose, D-mannose, D-glucosamine and ATP were 0.045, 4, 0.21, 0.05, 0.35 and 0.3 mM, respectively. N-Acetyl-D-glucosamine, D-xylose and D-galactose were not phosphorylated. The enzyme was strongly inhibited by the reaction products, glucose 6-phosphate and ADP, but not by high levels of D-glucose. The starfish hexokinase thus resembled mammalian isozyme A with respect to kinetic properties.
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PMID:Purification and properties of hexokinase from the starfish, Asterias amurensis. 89 76

Properties of hexokinase (EC 2.7.1.1) from Trypanosoma cruzi epimastigote forms (Tulahuen strain) were studied and compared with enzymes from other sources. The enzyme activity was 37 units g-1 of wet cells (1.2 units mg-1 protein). Hexokinase showed Km values for glucose and ATP of 0.09 and 0.4 mM, respectively. The enzyme reacted with other nucleotides too. N-Acetylglucosamine was a competitive inhibitor with respect to glucose (Ki = 0.3 mM). ADP inhibited the enzyme competitively with respect to ATP (Ki = 1.5 mM) and noncompetitively with respect to glucose (Ki = 7 mM). The enzyme was markedly inhibited by 5-thioglucose, its Ki value was 0.4 mM. Hexokinase activity was not affected by glucose 6-phosphate.
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PMID:Characterization of Trypanosoma cruzi hexokinase. 636 48