The enzyme, which has been purified from the bacteria Klebsiella oxytoca and Bacillus licheniformis, is part of a D-tagatose catabolic pathway. The substrate, which occurs in a pyranose form in solution, undergoes a change to the furanose conformation after binding to the enzyme, in order to permit phosphorylation at C-6.
The enzyme appears in viruses and cellular organisms
The enzyme, which has been purified from the bacteria Klebsiella oxytoca and Bacillus licheniformis, is part of a D-tagatose catabolic pathway. The substrate, which occurs in a pyranose form in solution, undergoes a change to the furanose conformation after binding to the enzyme, in order to permit phosphorylation at C-6.
Substrates: the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate. The catalytic efficiency of the enzyme for D-tagatose 1-phosphate is 40fold higher than that for fructose 1-phosphate, confirming that the enzyme is a D-tagatose 1-phosphate-specific kinase Products: -
Substrates: the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate. The catalytic efficiency of the enzyme for D-tagatose 1-phosphate is 40fold higher than that for fructose 1-phosphate, confirming that the enzyme is a D-tagatose 1-phosphate-specific kinase Products: -
Substrates: the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate Products: -
Substrates: the bifunctional enzyme shows phospho-tagatokinase and phospho-fructokinase activities, the latter with D-fructose-1-phosphate as substrate Products: -
Michaelis-Menten kinetics, the catalytic efficiency of the enzyme for D-tagatose 1-phosphate of 137.5 M/s is 40fold higher than that for fructose 1-phosphate with 3.4 M/s, confirming that the enzyme is a D-tagatose 1-phosphate-specific kinase
Van der Heiden, E.; Delmarcelle, M.; Simon, P.; Counson, M.; Galleni, M.; Freedberg, D.I.; Thompson, J.; Joris, B.; Battistel, M.D.
Synthesis and physicochemical characterization of D-tagatose-1-phosphate: the substrate of the tagatose-1-phosphate kinase in the phosphotransferase system-mediated D-tagatose catabolic pathway of catabolic pathway of Bacillus licheniformis
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