caa a22 4500 475743849 CHVBK 20180406123507.0 cr unu---uuuuu 170329e20000101xx s 000 0 eng 10.1023/A:1007099010762 doi (NATIONALLICENCE)springer-10.1023/A:1007099010762 Molecular Modeling of the Complexes between Saccharomyces cerevisiae Phosphoenolpyruvate Carboxykinase and the ATP Analogs Pyridoxal 5′-Diphosphoadenosine and Pyridoxal 5′-Triphosphoadenosine. Specific Labeling of Lysine 290 [Elektronische Daten] [Fernando González-Nilo, Rubén Vega, Emilio Cardemil] Molecular mechanics calculations have been employed to obtain models of the complexes between Saccharomyces cerevisiae phosphoenolpyruvate (PEP) kinase and the ATP analogs pyridoxal 5′-diphosphoadenosine (PLP-AMP) and pyridoxal 5′-triphosphoadenosine (PLP-ADP), using the crystalline coordinates of the ATP-pyruvate-Mn2+-Mg2+ complex of Escherichia coli PEP carboxykinase [Tari et al. (1997), Nature Struct. Biol. 4, 990-994]. In these models, the preferred conformation of the pyridoxyl moiety of PLP-ADP and PLP-AMP was established through rotational barrier and simulated annealing procedures. Distances from the carbonyl-C of each analog to ε-N of active-site lysyl residues were calculated for the most stable enzyme-analog complex conformation, and it was found that the closest ε-N is that from Lys290, thus predicting Schiff base formation between the corresponding carbonyl and amino groups. This prediction was experimentally verified through chemical modification of S. cerevisiae PEP carboxykinase with PLP-ADP and PLP-AMP. The results here described demonstrate the use of molecular modeling procedures when planning chemical modification of enzyme-active sites. Plenum Publishing Corporation, 2000 Homology modeling nationallicence rotational energy barrier nationallicence simulated annealing nationallicence pyridoxal 5′-diphosphoadenosine nationallicence pyridoxal 5′-triphosphoadenosine nationallicence Saccharomyces cerevisiae nationallicence phosphoenolpyruvate carboxykinase nationallicence González-Nilo Fernando Departamento de Ciencias Químicas, Facultad de Química y Biología, Universidad de Santiago de Chile, Casilla 40, Santiago 33, Chile aut Vega Rubén Departamento de Ciencias Químicas, Facultad de Química y Biología, Universidad de Santiago de Chile, Casilla 40, Santiago 33, Chile aut Cardemil Emilio Departamento de Ciencias Químicas, Facultad de Química y Biología, Universidad de Santiago de Chile, Casilla 40, Santiago 33, Chile aut Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/1(2000-01-01), 67-73 0277-8033 19:1<67 2000 19 10930 https://doi.org/10.1023/A:1007099010762 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1007099010762 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- González-Nilo Fernando Departamento de Ciencias Químicas, Facultad de Química y Biología, Universidad de Santiago de Chile, Casilla 40, Santiago 33, Chile aut NATIONALLICENCE 700 1- Vega Rubén Departamento de Ciencias Químicas, Facultad de Química y Biología, Universidad de Santiago de Chile, Casilla 40, Santiago 33, Chile aut NATIONALLICENCE 700 1- Cardemil Emilio Departamento de Ciencias Químicas, Facultad de Química y Biología, Universidad de Santiago de Chile, Casilla 40, Santiago 33, Chile aut NATIONALLICENCE 773 0- Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/1(2000-01-01), 67-73 0277-8033 19:1<67 2000 19 10930 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer