scholarly journals The structure of glycogen phosphorylase b with an alkyldihydropyridine-dicarboxylic acid compound, a novel and potent inhibitor

Structure ◽  
1997 ◽  
Vol 5 (11) ◽  
pp. 1413-1425 ◽  
Author(s):  
Spyros E Zographos ◽  
Nikos G Oikonomakos ◽  
Katerina E Tsitsanou ◽  
Demetrios D Leonidas ◽  
Evangelia D Chrysina ◽  
...  
1992 ◽  
Vol 45 (6) ◽  
pp. 1087 ◽  
Author(s):  
L Xin ◽  
NF Curtis

The (dimethyl trans-1,4,8,1l-tetraazacyclotetradecane-6,13-dicarboxylate)copper(II) cation reacts with ammonia, methylamine or hydrazine to give the dicarbamoyl-, di(methylcarbamoyl)- or di(hydrazinocarbonyl)-substituted complex cations, respectively. The 6,6,13,13-tetra(methoxy- carbonyl)-substituted compound reacts with ammonia at O�C to form the tetracarbamoyl- substituted macrocycle compound [which can also be prepared by condensation of bis(ethane-1,2-diamine)copper(II), formaldehyde and malondiamide], and the dicarbamoyl dicarboxylic acid compound at higher temperatures. Reaction of the tetra(ethoxycarbonyl) compound with ammonia yields a variety of products, depending upon conditions. Reaction of the tetra (ethoxycarbonyl) compound with methylamine yields the di(N- methylcarbamoyl) di(carboxy1ato) substituted macrocycle compound. Condensation of bis(ethane-1,2-diamine)copper(II), formaldehyde and N,N1-diethylmalondiamide yields the tetra(ethylcarbamoyl)-substituted macrocyle compound. A similar reaction with N,N1- dimethylmalondiamide yields a compound with a methylene group additional to the tetra(methylcarbamoyl) formulation.


1995 ◽  
Vol 308 (3) ◽  
pp. 1017-1023 ◽  
Author(s):  
I P Street ◽  
S G Withers

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.


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

2007 ◽  
Vol 72 (5) ◽  
pp. 518-528 ◽  
Author(s):  
A. V. Meremyanin ◽  
T. B. Eronina ◽  
N. A. Chebotareva ◽  
S. Yu. Kleimenov ◽  
I. K. Yudin ◽  
...  

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 ◽  
...  

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