Zobrazeno 1 - 10
of 71
pro vyhledávání: '"D., MEADOW"'
Autor:
Mariana Hávová, J B Doe, A B Smith, R D Meadow, Marie Sedlaříková, Adam Košíček, H B Hill, X.-Y. Xu, T R Price, Jiří Vondrák
Publikováno v:
ECS Transactions. 74:223-229
The research focused on samples of porous iron based materials. They were prepared by filing polyurethane foam with a mixture of iron and other metal powders (Ag, Mg and Si) and by annealing the samples in nitrogen atmosphere. Their fundamental behav
Publikováno v:
Journal of Biological Chemistry. 281:11450-11455
IIAGlc, a component of the glucose-specific phosphoenolpyruvate:phosphotransferase system (PTS) of Escherichia coli, is important in regulating carbohydrate metabolism. In Glc uptake, the phosphotransfer sequence is: phosphoenolpyruvate → Enzyme I
Publikováno v:
Journal of Biological Chemistry. 280:41872-41880
During translocation across the cytoplasmic membrane of Escherichia coli, glucose is phosphorylated by phospho-IIAGlc and Enzyme IICBGlc, the last two proteins in the phosphotransfer sequence of the phosphoenolpyruvate:glucose phosphotransferase syst
Publikováno v:
Journal of Bacteriology. 183:3336-3344
Reverse genetics is used to evaluate the roles in vivo of allosteric regulation of Escherichia coli glycerol kinase by the glucose-specific phosphocarrier of the phosphoenolpyruvate:glycose phosphotransferase system, IIA Glc (formerly known as III gl
Publikováno v:
The Journal of Physical Chemistry B. 105:2043-2055
We report an experimental study of protein relaxation dynamics on the picosecond and nanosecond time scales. The protein equilibrium state is perturbed by the redistribution of electric charge density over the side chain of a tryptophan residue. Elec
Publikováno v:
Biochemistry. 37:4875-4883
In Escherichia coli, inducer exclusion is one mechanism by which glucose prevents unnecessary expression of genes needed for metabolism of other sugars. The basis for this mechanism is binding of the unphosphorylated form of the glucose-specific phos
Publikováno v:
Biochemistry. 36:16087-16096
In Escherichia coli, the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS), IIAGlc (IIIGlc in older literature), is also the central regulatory protein of the PTS. Depending upon its state of phosphorylation, IIAGlc binds
Autor:
S. James Remington, Dennis A. Torchia, Saul Roseman, Norman D. Meadow, Kenneth P. Murphy, Jeffrey G. Pelton
Publikováno v:
Journal of Biological Chemistry. 271:33446-33456
IIIGlc (also called IIAGlc), a major signal-transducing protein in Escherichia coli, is also a phosphorylcarrier in glucose uptake. The crystal and NMR structures of IIIGlc show that His90, the phosphoryl acceptor, adjoins His75 in the active site. G
Publikováno v:
Protein Science. 2:543-558
IIIGlc is an 18.1-kDa signal-transducing phosphocarrier protein of the phosphoenolpyruvate:glycose phosphotransferase system from Escherichia coli. The 1H, 15N, and 13C histidine ring NMR signals of both the phosphorylated and unphosphorylated forms
Publikováno v:
Biochemistry. 31:5215-5224
The 18.1-kDa protein IIIGlc from Escherichia coli acts as both a phosphocarrier protein in the phosphoenolpyruvate:glycose phosphotransferase system (PTS) and as a signal-transducing protein with respect to the uptake of non-PTS sugars. Phosphorylati