Effect of metabolites and phosphorylase on the D to I conversion of glycogen synthase from human polymorphonuclear leukocytes.

  title={Effect of metabolites and phosphorylase on the D to I conversion of glycogen synthase from human polymorphonuclear leukocytes.},
  author={P Wang and G. Bantle and N B Sorensen},
  journal={Biochimica et biophysica acta},
  volume={496 2},
6 Citations

The hysteretic properties of glycogen synthase I.

Evidence from ultracentrifugation and kinetic studies is presented to substantiate the hypothesis that the underlying mechanism is a simple biolecular process: enzyme + glycogen in equilibrium enzyme-glycogen complex, with the dissociation constant Ks = 0.003 mg/ml.

Studies on the allosteric properties of glycogen synthase I.

It is concluded that glycogen synthase I is subject to allosteric control and under physiological conditions is not always fully active.

A continuous assay method for glycogen synthesis from UDPglucose.

The effect of glucose and glucose analogues on the conversion of glycogen synthetase from phosphorylated to dephosphorylated form in human polymorphonuclear leukocytes.

Incubation of human polymorphonuclear leukocytes in a glucose-free buffer resulted in a large decrease in glycogen content and phosphorylase activity and a D to I conversion, which persisted, in contrast to the activation obtained with glucose.

Inactivation of glycogen phosphorylase of human polymorphonuclear leukocytes.

It is concluded that the phosphorylase of human polymorphonuclear leukocytes is closely related to liver phosphoryLase and that the inactivation of the enzyme is mainly controlled by AMP and glucose.

The influence of inorganic phosphate, adenosine triphosphate and glucose 6-phosphate on the activity of liver glycogen synthetase.

In the cell, Pi appears to be the most important activator of the enzyme, whereas glucose 6-phosphate has only a minor role.

Glycogen synthetase-D phosphatase. I. Some new properties of the partially purified enzyme from rabbit skeletal muscle.

Findings suggest that these two phosphatase activities may reside in the same enzyme protein, and are found to be optimal compared to the slower reaction rates found with greater or lesser concentrations.

The control of liver glycogen synthetase phosphatase by phosphorylase.

It has been shown that the dose of glycogen that prolongs the lag period also inhibits phosphorylase posphatase, wherease AMP and magnesium counteract the inhibition of synthetase phosphatase by phosphoryLase a.

Purification and properties of rabbit-liver glycogen synthase.

Glycogen synthase b was purified from rabbit liver by a procedure involving isolation of the glycogen-enzyme complex, DEAE-cellulose chromatography, and affinity chromatography and appeared to be homogeneous by the criterion of polyacrylamide disc gel electrophoresis.

Rat adipose tissue glycogen synthase. Evidence for multiple discrete kinetic species and their interconversion.

  • R. Eichner
  • Biology, Chemistry
    The Journal of biological chemistry
  • 1976
Rat adipose tissue glycogen synthase has been kinetically characterized. The classical D form has an apparent Km for UDP-glucose of 0.7 mM and 0.4 mM in the absence and presence of glucose

Structure and Regulation of Enzymes for the Degradation and Resynthesis of Glycogen

Substrate analogues with an epoxide function have been found to be the most effective inhibitors for glycosidases, and here too the covalent reaction is catalysed by an acidic group at the active site that protonates the epoxide and makes it more reactive.