AAAAAA

   
Results: 1-7 |
Results: 7
Substitution of aspartate and glutamate for active center histidines in the Escherichia coli phosphoenolpyruvate : sugar phosphotransferase system maintain phosphotransfer potential
Authors: Napper, S Brokx, SJ Pally, E Kindrachuk, J Delbaere, LTJ Waygood, EB
Citation: S. Napper et al., Substitution of aspartate and glutamate for active center histidines in the Escherichia coli phosphoenolpyruvate : sugar phosphotransferase system maintain phosphotransfer potential, J BIOL CHEM, 276(45), 2001, pp. 41588-41593
Enzyme I of the phosphoenolpyruvate : sugar phosphotransferase system. In vitro intragenic complementation: The roles of Arg126 in phosphoryl transfer and the C-terminal domain in dimerization
Authors: Brokx, SJ Talbot, J Georges, F Waygood, EB
Citation: Sj. Brokx et al., Enzyme I of the phosphoenolpyruvate : sugar phosphotransferase system. In vitro intragenic complementation: The roles of Arg126 in phosphoryl transfer and the C-terminal domain in dimerization, BIOCHEM, 39(13), 2000, pp. 3624-3635
Identification of the Escherichia coli enzyme I binding site in histidine-containing protein, HPr, by the effects of mutagenesis
Authors: Brokx, SJ Napper, S Wong, G Mirza, A Georges, F Delbaere, LTJ Waygood, EB
Citation: Sj. Brokx et al., Identification of the Escherichia coli enzyme I binding site in histidine-containing protein, HPr, by the effects of mutagenesis, BIOC CELL B, 77(6), 1999, pp. 507-513
Synthesis, cloning and expression of the single-chain Fv gene of the HPr-specific monoclonal antibody, Jel42. Determination of binding constants withwild-type and mutant HPrs
Authors: Smallshaw, JE Georges, F Lee, JS Waygood, EB
Citation: Je. Smallshaw et al., Synthesis, cloning and expression of the single-chain Fv gene of the HPr-specific monoclonal antibody, Jel42. Determination of binding constants withwild-type and mutant HPrs, PROTEIN ENG, 12(7), 1999, pp. 623-630
The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli phosphoenolpyruvate: Sugar phosphotransferase system can accept and donate a phosphoryl group - Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization
Authors: Napper, S Delbaere, LTJ Waygood, EB
Citation: S. Napper et al., The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli phosphoenolpyruvate: Sugar phosphotransferase system can accept and donate a phosphoryl group - Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization, J BIOL CHEM, 274(31), 1999, pp. 21776-21782
The structure and function of HPr
Authors: Waygood, EB
Citation: Eb. Waygood, The structure and function of HPr, BIOC CELL B, 76(2-3), 1998, pp. 359-367
Conversion of an antibody into an enzyme which cleaves the protein HPr
Authors: Liu, E Prasad, L Delbaere, LTJ Waygood, EB Lee, JS
Citation: E. Liu et al., Conversion of an antibody into an enzyme which cleaves the protein HPr, MOL IMMUNOL, 35(16), 1998, pp. 1069-1077
Risultati: 1-7 |