Results 81 to 90 of about 12,748,427 (99)
De Novo Assembly and Analysis of Polygonatum sibiricum Transcriptome and Identification of Genes Involved in Polysaccharide Biosynthesis. [PDF]
Int J Mol Sci, 2017 Wang S +6 more
europepmc +1 more source
Udpglucose 4-epimerase from Saccharomyces fragilis: Desensitization with heat
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.
Manju Ray, Amar Bhaduri, A Bhaduri
exaly +4 more sources
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.
Manju Ray, Amar Bhaduri, A Bhaduri
exaly +4 more sources
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Two forms of UDPglucose-4-epimerase from mammalian liver
Biochimica Et Biophysica Acta - Biomembranes, 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
Manju Ray, Amar Bhaduri, A Bhaduri
exaly +3 more sources
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
Manju Ray, Amar Bhaduri, A Bhaduri
exaly +3 more sources
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
Manju Ray, Amar Bhaduri, A Bhaduri
exaly +3 more sources
Nucleotide inhibition of udpglucose 4-epimerase from Saccharomyces fragilis and from goat liver
Biochimica Et Biophysica Acta - Biomembranes, 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.
Amar Bhaduri, A Bhaduri
exaly +2 more sources
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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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
Identification and Characterization of a Mutation, in the Human UDP-Galactose-4-Epimerase Gene, Associated with Generalized Epimerase-Deficiency Galactosemia [PDF]
American Journal of Human Genetics, 1999 SummaryEpimerase-deficiency galactosemia results from impairment of the human enzyme UDP-galactose-4-epimerase (hGALE). We and others have identified substitution mutations in the hGALE alleles of patients with the clinically mild, peripheral form of ...
Judith Fridovich-Keil +1 more
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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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