caa a22 4500 475744187 CHVBK 20180406123508.0 cr unu---uuuuu 170329e20000401xx s 000 0 eng 10.1023/A:1007055719926 doi (NATIONALLICENCE)springer-10.1023/A:1007055719926 Analysis of Aluminum—Yeast Hexokinase Interaction: Modifications on Protein Structure and Functionality [Elektronische Daten] [J. Socorro, R. Olmo, C. Teijón, M. Blanco, J. Teijón] The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first concentration). At large salt concentrations a monomerization process and a conformational change in the secondary structure as well as in the three-dimensional structure take place. This change reduces the percentage of α-helix conformation, gives thermal stability to the protein, and allows the exposure of some tryptophan residue and hydrophobic regions. The protein inhibition increases. Conformational change and monomerization may allow access of the metal to the substrate site, mainly the ATP site. The inhibition in any case is of mixed type with a competitive component. Plenum Publishing Corporation, 2000 Aluminum nationallicence yeast hexokinase nationallicence preferential interactions nationallicence kinetics nationallicence Socorro J. Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Complutense de Madrid, 28040, Madrid, Spain aut Olmo R. Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Complutense de Madrid, 28040, Madrid, Spain aut Teijón C. Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Complutense de Madrid, 28040, Madrid, Spain aut Blanco M. Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Complutense de Madrid, 28040, Madrid, Spain aut Teijón J. Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Complutense de Madrid, 28040, Madrid, Spain aut Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/3(2000-04-01), 199-208 0277-8033 19:3<199 2000 19 10930 https://doi.org/10.1023/A:1007055719926 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1007055719926 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Socorro J. Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Complutense de Madrid, 28040, Madrid, Spain aut NATIONALLICENCE 700 1- Olmo R. Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Complutense de Madrid, 28040, Madrid, Spain aut NATIONALLICENCE 700 1- Teijón C. Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Complutense de Madrid, 28040, Madrid, Spain aut NATIONALLICENCE 700 1- Blanco M. Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Complutense de Madrid, 28040, Madrid, Spain aut NATIONALLICENCE 700 1- Teijón J. Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Complutense de Madrid, 28040, Madrid, Spain aut NATIONALLICENCE 773 0- Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/3(2000-04-01), 199-208 0277-8033 19:3<199 2000 19 10930 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer