Sequence of the carboxyl-terminal 492 residues of rabbit muscle glycogen phosphorylase including the pyridoxal 5'-phosphate binding site

Biochemistry ◽  
1978 ◽  
Vol 17 (26) ◽  
pp. 5680-5695 ◽  
Author(s):  
Koite Titani ◽  
Atsushi Koide ◽  
Lowell H. Ericsson ◽  
Santosh Kumar ◽  
Jacques Hermann ◽  
...  
Keyword(s):  
Binding Site ◽  
Muscle Glycogen ◽  
Glycogen Phosphorylase ◽  
Rabbit Muscle ◽  
Phosphate Binding ◽  
Carboxyl Terminal

Sequence of a segment of muscle glycogen phosphorylase containing the pyridoxal 5'-phosphate binding site

Biochemistry ◽  
1971 ◽  
Vol 10 (16) ◽  
pp. 3132-3140 ◽  
Author(s):  
Edmond H. Fischer ◽  
Arden W. Forrey ◽  
Cynthia L. Sevilla ◽  
John C. Saari
Keyword(s):  
Binding Site ◽  
Muscle Glycogen ◽  
Glycogen Phosphorylase ◽  
Phosphate Binding

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.

Temperature-sensitive production of rabbit muscle glycogen phosphorylase in Escherichia coli

1991 ◽  
Vol 4 (3) ◽  
pp. 351-357 ◽  
Author(s):  
Michelle F. Browner ◽  
Peter Rasor ◽  
Stuart Tugendreich ◽  
Robert J. Fletterick
Keyword(s):  
Escherichia Coli ◽  
Muscle Glycogen ◽  
Glycogen Phosphorylase ◽  
Temperature Sensitive ◽  
Rabbit Muscle

scholarly journals Complete cDNA sequence for rabbit muscle glycogen phosphorylase

FEBS Letters ◽  
1986 ◽  
Vol 204 (2) ◽  
pp. 283-287 ◽  
Author(s):  
Kenichi Nakano ◽  
Peter K. Hwang ◽  
Robert J. Fletterick
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Phosphorylase ◽  
Cdna Sequence ◽  
Rabbit Muscle

scholarly journals Allosteric interactions of glycogen phosphorylase b. A crystallographic study of glucose 6-phosphate and inorganic phosphate binding to di-imidate-cross-linked phosphorylase b

1984 ◽  
Vol 218 (1) ◽  
pp. 45-60 ◽  
Author(s):  
A Lorek ◽  
K S Wilson ◽  
M S P Sansom ◽  
D I Stuart ◽  
E A Stura ◽  
...  
Keyword(s):  
Binding Site ◽  
Conformational Changes ◽  
Inorganic Phosphate ◽  
Glycogen Phosphorylase ◽  
Phosphate Binding ◽  
Binding Studies ◽  
Structural Explanation ◽  
Alpha Helices ◽  
Allosteric Effector ◽  
Glycogen Phosphorylase B

The binding to glycogen phosphorylase b of glucose 6-phosphate and inorganic phosphate (respectively allosteric inhibitor and substrate/activator of the enzyme) were studied in the crystal at 0.3 nm (3A) resolution. Glucose 6-phosphate binds in the alpha-configuration at a site that is close to the AMP allosteric effector site at the subunit-subunit interface and promotes several conformational changes. The phosphate-binding site of the enzyme for glucose 6-phosphate involves contacts to two cationic residues, Arg-309 and Lys-247. This site is also occupied in the inorganic-phosphate-binding studies and is therefore identified as a high-affinity phosphate-binding site. It is distinct from the weaker phosphate-binding site of the enzyme for AMP, which is 0.27 nm (2.7A) away. The glucose moiety of glucose 6-phosphate and the adenosine moiety of AMP do not overlap. The results provide a structural explanation for the kinetic observations that glucose 6-phosphate inhibition of AMP activation of phosphorylase b is partially competitive and highly co-operative. The results suggest that the transmission of allosteric conformational changes involves an increase in affinity at phosphate-binding sites and relative movements of alpha-helices. In order to study glucose 6-phosphate and phosphate binding it was necessary to cross-link the crystals. The use of dimethyl malondi-imidate as a new cross-linking reagent in protein crystallography is discussed.

Probing the catalytic site of rabbit muscle glycogen phosphorylase using a series of specifically modified maltohexaose derivatives

2017 ◽  
Vol 34 (4) ◽  
pp. 563-574 ◽  
Author(s):  
Makoto Nakamura ◽  
Yasushi Makino ◽  
Chika Takagi ◽  
Tohru Yamagaki ◽  
Masaaki Sato
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Phosphorylase ◽  
Catalytic Site ◽  
Rabbit Muscle
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