scholarly journals The Anomeric Specificity of Enzymes Which Act on Sugars

2007 ◽  
Vol 84 (10) ◽  
pp. 1608 ◽  
Author(s):  
E. J. Behrman ◽  
Venkat Gopalan
Keyword(s):  
Anomeric Specificity

Anomeric Specificity of Human Liver and B-cell Glucokinase: Modulation by the Glucokinase Regulatory Protein

2000 ◽  
Vol 373 (1) ◽  
pp. 126-134 ◽  
Author(s):  
Philippe Courtois ◽  
Frédéric Bource ◽  
Abdullah Sener ◽  
Willy J. Malaisse
Keyword(s):  
B Cell ◽  
Human Liver ◽  
Regulatory Protein ◽  
Glucokinase Regulatory Protein ◽  
Anomeric Specificity

scholarly journals Anomeric specificity of d-glucose phosphorylation by rat liver glucose-6-phosphatase

1989 ◽  
Vol 261 (2) ◽  
pp. 509-513
Author(s):  
R Ramirez ◽  
D Zähner ◽  
G Marynissen ◽  
A Sener ◽  
W J Malaisse
Keyword(s):  
Rat Liver ◽  
Glycogen Synthesis ◽  
Liver Microsomes ◽  
Diabetic Rats ◽  
Enzymic Activity ◽  
Rat Liver Microsomes ◽  
Maximal Velocity ◽  
Carbamoyl Phosphate ◽  
Glucose Phosphorylation ◽  
Anomeric Specificity

The anomeric specificity of D-glucose phosphorylation by hepatic glucose-6-phosphatase was examined in rat liver microsomes incubated in the presence of carbamoyl phosphate. At 10 degrees C, the Km for the equilibrated hexose and phosphate donor was close to 56 mM and 11 mM, respectively. The enzymic activity, which was increased in diabetic rats, was about 40% lower in untreated than in sonicated microsomes. No anomeric difference in affinity was found in sonicated microsomes. In untreated microsomes, however, the Km for beta-D-glucose was slightly lower than that for alpha-D-glucose. The maximal velocity was higher with beta- than alpha-D-glucose in both untreated and sonicated microsomes. These data indicate that the phosphotransferase activity of glucose-6-phosphatase cannot account for the higher rate of glycolysis and glycogen synthesis found in hepatocytes exposed to alpha- rather than beta-D-glucose.

Carbon-13 NMR investigation of the anomeric specificity of CMP-N-acetylneuraminic acid synthetase from Escherichia coli

Biochemistry ◽  
1992 ◽  
Vol 31 (3) ◽  
pp. 775-780 ◽  
Author(s):  
Michael G. Ambrose ◽  
Stephen J. Freese ◽  
Mary S. Reinhold ◽  
Thomas G. Warner ◽  
Willie F. Vann
Keyword(s):  
Escherichia Coli ◽  
Acetylneuraminic Acid ◽  
Anomeric Specificity

Anomeric specificity of hexose metabolism in pancreatic islets

1983 ◽  
Vol 63 (3) ◽  
pp. 773-786 ◽  
Author(s):  
W. J. Malaisse ◽  
F. Malaisse-Lagae ◽  
A. Sener
Keyword(s):  
Pancreatic Islets ◽  
Anomeric Specificity ◽  
Hexose Metabolism

The anomeric specificity of β-galactosidase and lac permease from Escherichia coli

1981 ◽  
Vol 59 (2) ◽  
pp. 100-105 ◽  
Author(s):  
R. E. Huber ◽  
K. L. Hurlburt ◽  
C. L. Turner
Keyword(s):  
Escherichia Coli ◽  
Glycosidic Bond ◽  
Lac Operon ◽  
Acceptor Reaction ◽  
Glucose Release ◽  
Bond Breakage ◽  
Lactose Metabolism ◽  
Anomeric Specificity

β-Galactosidase was found to act on α-lactose slightly more than twice as rapidly as on β-lactose for both the hydrolysis and transgalactosylis reactions. The effect was shown to be on the Vmax values; the Km values for the different anomeric forms were the same. The step of the reaction for which the enzyme has anomeric specificity was shown to be glycosidic bond breakage. The steps in glucose release or in the glucose acceptor reaction were not affected by anomeric composition. Neither allolactose hydrolysis nor transport of lactose into the cells by lac permease was sensitive to the anomeric composition of the substrate. The implications of these results for lac operon induction and for lactose metabolism are discussed.

Anomeric Specificity of Glucose-Stimulated Insulin Release: Evidence for a Glucoreceptor?

Science ◽  
1974 ◽  
Vol 186 (4163) ◽  
pp. 536-538 ◽  
Author(s):  
G. M. Grodsky ◽  
R. Fanska ◽  
L. West ◽  
M. Manning
Keyword(s):  
Insulin Release ◽  
Anomeric Specificity
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