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Results: 1-4 |
Results: 4
Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae
Authors: Samland, AK Etezady-Esfarjani, T Amrhein, N Macheroux, P
Citation: Ak. Samland et al., Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae, BIOCHEM, 40(6), 2001, pp. 1550-1559
Thermodynamic characterization of ligand-induced conformational changes inUDP-N-acetylglucosamine enolpyruvyl transferase
Authors: Samland, AK Jelesarov, I Kuhn, R Amrhein, N Macheroux, P
Citation: Ak. Samland et al., Thermodynamic characterization of ligand-induced conformational changes inUDP-N-acetylglucosamine enolpyruvyl transferase, BIOCHEM, 40(33), 2001, pp. 9950-9956
Determination of the pK(a) value of C115 in MurA (UDP-N-acetylglucosamine enolpyruvyltransferase) from Enterobacter cloacae
Authors: Krekel, F Samland, AK Macheroux, P Amrhein, N Evans, JNS
Citation: F. Krekel et al., Determination of the pK(a) value of C115 in MurA (UDP-N-acetylglucosamine enolpyruvyltransferase) from Enterobacter cloacae, BIOCHEM, 39(41), 2000, pp. 12671-12677
Lysine 22 in UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae is crucial for enzymatic activity and the formation of covalent adducts with the substrate phosphoenolpyruvate and the antibiotic fosfomycin
Authors: Samland, AK Amrhein, N Macheroux, P
Citation: Ak. Samland et al., Lysine 22 in UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae is crucial for enzymatic activity and the formation of covalent adducts with the substrate phosphoenolpyruvate and the antibiotic fosfomycin, BIOCHEM, 38(40), 1999, pp. 13162-13169
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