Results 91 to 100 of about 314 (108)
Udpglucose 4-epimerase from Saccharomyces fragilis: Desensitization with heat [PDF]
Biochemical and Biophysical Research Communications, 1975 The allosteric kinetics exhibited by UDP glucose 4-epimerase from Saccharomyces fragilis changes over to a normal hyperbolic kinetics when the enzyme is heated at 41° for 2 mins. The native enzyme is completely insensitive to inhibition by UMP in the allosteric region.
M, Ray, A, Bhaduri
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Udpglucose-4 epimerase from Saccharomyces fragilis: Interaction with sugar phosphates at an effector site [PDF]
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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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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The presence of elements of a dinucleotide fold in UDP-glucose 4-epimerase from saccharomyces fragilis [PDF]
BBA - Proteins and Proteomics, 1982 UDPglucose 4-epimerase (EC 5.1.3.2) from Saccharomyces fragilis is a holoenzyme containing 1 mol NAD per mol dimeric protein. The enzyme can be dissociated with p-chloromercuribenzoate and can be reconstituted in the presence of 2-mercaptoethanol and ...
Amar Bhaduri, A Bhaduri
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UDP-Glucose 4-epimerase from Saccharomyces fragilis. Involvement of sulfhydryl group(s) at the active site [PDF]
Biochimica Et Biophysica Acta - Biomembranes, 1978 UDPglucose 4-epimerase (EC 5.1.3.2) from Saccharomyces fragilis is inactivated by 0.1 mM 5,5'-dithiobis-(2-nitrobenzoate) in 6 min. Unlike p-chloromercuribenzoate-inactivated or heat-inactivated enzymes, the dithiobisnitrobenzoate-inactivated enzyme ...
Manju Ray, Amar Bhaduri, A 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
openaire +2 more sources
Nucleotide inhibition of UDPglucose 4 4 -epimerase from Saccharomyces fragilis and from goat liver.
Biochimica et biophysica acta, 1972D K, Pal, A, Bhaduri
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Purification and Properties of Uridine Diphosphoglucose 4-epimerase from Escherichia coli*
Journal of Biochemistry, 1964Kiyoshi Kurahashi +2 more
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