Results 111 to 120 of about 2,141 (127)
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Two forms of UDPglucose-4-epimerase from mammalian liver
Biochimica et Biophysica Acta (BBA) - Enzymology, 1973Abstract UDPglucose-4-epimerase (EC 5.1.3.2) is shown to exist in two distinct forms in goat and beef liver. The two forms can be distinguished easily by their interaction with sugar phosphates and with substrate. The minor form comprising about 20% of the total activity, is activated by both Gal - i -P and Gal-6-P and is partially inhibited
M, Ray, A, Bhaduri
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Biochemical and Biophysical Research Communications, 1978
Summary UDPglucose 4-epimerase from Saccharomyces fragilis shows Michaelis kinetics with UDPgalactose as the substrate and allosteric kinetics with UDPglucose as the substrate. As a result of this allosteric asymmetry, when very low concentration of UDPgalactose is used as the substrate, a unidirectional catalysis takes place and the equilibrium is
M, Ray, A, Bhaduri
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Summary UDPglucose 4-epimerase from Saccharomyces fragilis shows Michaelis kinetics with UDPgalactose as the substrate and allosteric kinetics with UDPglucose as the substrate. As a result of this allosteric asymmetry, when very low concentration of UDPgalactose is used as the substrate, a unidirectional catalysis takes place and the equilibrium is
M, Ray, A, Bhaduri
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Nucleotide inhibition of udpglucose 4-epimerase from Saccharomyces fragilis and from goat liver
Biochimica et Biophysica Acta (BBA) - Enzymology, 1971Abstract UDPglucose 4-epimerase (EC 5.1.3.2) from both goat liver and the yeast Saccharomyces fragilis was strongly inhibited by uridine nucleotides. The yeast enzyme, unlike the liver one, showed substrate inhibition. UMP, in combination with various sugars, slowly but irreversibly inactivated the yeast enzyme.
Dilip K. Pal, Amar Bhaduri
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Biochimica et Biophysica Acta (BBA) - Enzymology, 1975
1. The specific activity of UDPglucose 4-epimerase (EC 5.1.3.2) increases by about 50% during the first 24 h of starvation-induced differentiation (spherulation) of Physarum polycephalum. 2. At all stages during differentiation, the enzyme activity is very sensitive to actinomycin-C and cycloheximide, inhibitors of transcription and translation, with a
A, Hüttermann +3 more
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1. The specific activity of UDPglucose 4-epimerase (EC 5.1.3.2) increases by about 50% during the first 24 h of starvation-induced differentiation (spherulation) of Physarum polycephalum. 2. At all stages during differentiation, the enzyme activity is very sensitive to actinomycin-C and cycloheximide, inhibitors of transcription and translation, with a
A, Hüttermann +3 more
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Biochemical and Biophysical Research Communications, 1974
UDP glucose-4 epimerase from Saccharomyces fragilis was found to be activated at low substrate concentrations by some metabolically related sugar phosphates. The stimulation of the enzyme activity showed a sigmoidal response to the increasing concentration of glucose-6 phosphate at a fixed substrate concentration.
M, Ray, A, Bhaduri
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UDP glucose-4 epimerase from Saccharomyces fragilis was found to be activated at low substrate concentrations by some metabolically related sugar phosphates. The stimulation of the enzyme activity showed a sigmoidal response to the increasing concentration of glucose-6 phosphate at a fixed substrate concentration.
M, Ray, A, Bhaduri
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, 2020
d-Tagatose, a low-calorie functional sweetener, is biotransformed from lactose via galactose. The discovery of an enzyme with 4-epimerization activity toward d-fructose to produce d-tagatose has be...
K. Shin +5 more
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d-Tagatose, a low-calorie functional sweetener, is biotransformed from lactose via galactose. The discovery of an enzyme with 4-epimerization activity toward d-fructose to produce d-tagatose has be...
K. Shin +5 more
semanticscholar +1 more source
Journal of Agricultural and Food Chemistry
d-Tagatose, a rare sugar endowed with a low-calorie property, superior taste quality, and probiotic functionality, has garnered significant research attention.
Zhanzhi Liu +3 more
semanticscholar +1 more source
d-Tagatose, a rare sugar endowed with a low-calorie property, superior taste quality, and probiotic functionality, has garnered significant research attention.
Zhanzhi Liu +3 more
semanticscholar +1 more source
Protein Engineering of Tagatose 4-Epimerase for D-Tagatose Production.
Journal of Agricultural and Food ChemistryD-Tagatose, a promising sugar substitute with various functional properties and commercial applications, can be enzymatically converted from D-fructose by tagatose 4-epimerase.
Yuxin Wang +7 more
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Journal of Agricultural and Food Chemistry
d-Tagatose is a highly promising functional sweetener known for its various physiological functions. In this study, a novel tagatose 4-epimerase from Thermoprotei archaeon (Thar-T4Ease), with the ability to convert d-fructose to d-tagatose, was ...
Jiajun Chen +6 more
semanticscholar +1 more source
d-Tagatose is a highly promising functional sweetener known for its various physiological functions. In this study, a novel tagatose 4-epimerase from Thermoprotei archaeon (Thar-T4Ease), with the ability to convert d-fructose to d-tagatose, was ...
Jiajun Chen +6 more
semanticscholar +1 more source