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pro vyhledávání: '"Angeliki E. Melpidou"'
Uridine(5')Diphospho(1)-Alpha-D-Glucose - a Binding Study to Glycogen Phosphorylase-B in the Crystal
Autor:
David I. Stuart, P.J. McLaughlin, Nikos G. Oikonomakos, Louise N. Johnson, K. Ravindra Acharya, Angeliki E. Melpidou
Publikováno v:
European Journal of Biochemistry 173:3(May1988):569-578
UDP-glucose is an R-state inhibitor of glycogen phosphorylase b, competitive with the substrate, glucose 1-phosphate and noncompetitive with the allosteric activator, AMP. Diffusion of 100 mM UDP-glucose into crystals of phosphorylase b resulted in a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65c595cb77071902079b910278190c69
http://helios-eie.ekt.gr/EIE/handle/10442/2771
http://helios-eie.ekt.gr/EIE/handle/10442/2771
Publikováno v:
Archives of biochemistry and biophysics. 270(1)
The binding of β-glycerophosphate (glycerol-2-P) to glycogen phosphorylase b in the crystal has been studied by X-ray diffraction at 3 A resolution. Glycerol-2-P binds to the allosteric effector site in a position close to that of AMP, glucose-6-P,
Publikováno v:
Biochimica et biophysica acta. 832(3)
A new method for purification and crystallization of pig skeletal muscle phosphorylase b is presented. The ease of crystallization in the presence of 1 mM AMP and 1 mM spermine has permitted the study of some physical, chemical and enzymatic properti
Publikováno v:
FEBS letters. 154(1)
Kinetic studies of muscle phosphorylase a in cationic buffer (pH 6.8) demonstrate that glucose-6-P competitively inhibits the binding of the substrate, glucose-1-P, to the enzyme. The inhibitory effect of glucose-6-P is largely overcome by glycerol-2