scholarly journals The binding of β- and γ-cyclodextrins to glycogen phosphorylase b: Kinetic and crystallographic studies

2003 ◽  
Vol 12 (9) ◽  
pp. 1914-1924 ◽  
Author(s):  
Nikos Pinotsis ◽  
Demetres D. Leonidas ◽  
Evangelia D. Chrysina ◽  
Nikos G. Oikonomakos ◽  
Irene M. Mavridis
Keyword(s):  
Glycogen Phosphorylase ◽  
Glycogen Phosphorylase B

scholarly journals Probing the ionization state of substrate α-d-glucopyranosyl phosphate bound to glycogen phosphorylase b

1995 ◽  
Vol 308 (3) ◽  
pp. 1017-1023 ◽  
Author(s):  
I P Street ◽  
S G Withers
Keyword(s):  
Active Site ◽  
Glycogen Phosphorylase ◽  
Ph Dependence ◽  
Substrate Inhibition ◽  
19F Nmr ◽  
Ionization State ◽  
Nmr Studies ◽  
Substrate Analogues ◽  
Glycogen Phosphorylase B ◽  
Pka Value

The ionization state of the substrate alpha-D-glucopyranosyl phosphate bound at the active site of glycogen phosphorylase has been probed by a number of techniques. Values of Ki determined for a series of substrate analogue inhibitors in which the phosphate moiety bears differing charges suggest that the enzyme will bind both the monoanionic and dianionic substrates with approximately equal affinity. These results are strongly supported by 31P- and 19F-NMR studies of the bound substrate analogues alpha-D-glucopyranosyl 1-methylenephosphonate and 2-deoxy-2-fluoro-alpha-D-glucopyranosyl phosphate, which also suggest that the substrate can be bound in either ionization state. The pH-dependences of the inhibition constants K1 for these two analogues, which have substantially different phosphate pK2 values (7.3 and 5.9 respectively), are found to be essentially identical with the pH-dependence of K(m) values for the substrate, inhibition decreasing according to an apparent pKa value of 7.2. This again indicates that there is no specificity for monoanion or dianion binding and also reveals that binding is associated with the uptake of a proton. As the bound substrate is not protonated, this proton must be taken up by the proton.

Effect of α-crystallin on thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle

2007 ◽  
Vol 72 (5) ◽  
pp. 518-528 ◽  
Author(s):  
A. V. Meremyanin ◽  
T. B. Eronina ◽  
N. A. Chebotareva ◽  
S. Yu. Kleimenov ◽  
I. K. Yudin ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glycogen Phosphorylase ◽  
Rabbit Skeletal Muscle ◽  
Thermal Aggregation ◽  
Glycogen Phosphorylase B

Effect of 2-hydroxypropyl-β-cyclodextrin on thermal stability and aggregation of glycogen phosphorylase b from rabbit skeletal muscle

Biopolymers ◽  
2010 ◽  
Vol 93 (11) ◽  
pp. 986-993 ◽  
Author(s):  
Tatyana B. Eronina ◽  
Natalia A. Chebotareva ◽  
Sergey Yu. Kleymenov ◽  
Svetlana G. Roman ◽  
Valentina F. Makeeva ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Thermal Stability ◽  
Glycogen Phosphorylase ◽  
Rabbit Skeletal Muscle ◽  
Glycogen Phosphorylase B

AMP interaction sites in glycogen phosphorylase b A thermodynamic analysis

1985 ◽  
Vol 21 (3-4) ◽  
pp. 249-260 ◽  
Author(s):  
Margarita Menendez ◽  
Dolores Solis ◽  
Pilar Usobiaga ◽  
José Laynez
Keyword(s):  
Thermodynamic Analysis ◽  
Glycogen Phosphorylase ◽  
Interaction Sites ◽  
Glycogen Phosphorylase B

scholarly journals The nature of the binding site for aromatic compounds in glycogen phosphorylase b

1975 ◽  
Vol 147 (2) ◽  
pp. 369-371 ◽  
Author(s):  
G Soman ◽  
G Philip
Keyword(s):  
Chemical Modification ◽  
Binding Site ◽  
Aromatic Compounds ◽  
Glycogen Phosphorylase ◽  
Relative Effectiveness ◽  
Rabbit Muscle ◽  
Substituent Constant ◽  
Chemically Modified ◽  
Glycogen Phosphorylase B ◽  
Hydrophobic Nature

The inhibition of rabbit muscle glycogen phosphorylase b (1,4-alpha-D-glucan--orthophosphate alpha-glucosyltransferase, EC 2.4.1.1) by aromatic compounds was examined with 15 compounds. The relative effectiveness of the inhibitors correlated well with increasing substituent constant, pi, indicating the hydrophobic nature of the binding site. The inhibition was not affected by the ionic-strength variation of the assay mixtures. The results predict that the course of chemical modification of this enzyme and the properties of the derivatives depend on the nature of the reagent and on the incorporated groups. Many of the dissimilar and sometimes contradictory results reported for chemical-modification studies and for chemically modified phosphorylase b are explained by the findings presented in the paper.

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