Channels at the catalytic site of glycogen phosphorylase b: binding and kinetic studies with the .beta.-glycosidase inhibitor D-gluconohydroximo-1,5-lactone N-phenylurethane

Biochemistry ◽  
1988 ◽  
Vol 27 (18) ◽  
pp. 6733-6741 ◽  
Author(s):  
D. Barford ◽  
J. W. R. Schwabe ◽  
N. G. Oikonomakos ◽  
K. R. Acharya ◽  
J. Hajdu ◽  
...  
Keyword(s):  
Glycogen Phosphorylase ◽  
Kinetic Studies ◽  
Catalytic Site ◽  
Glycogen Phosphorylase B ◽  
Glycosidase Inhibitor

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.

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

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
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