Abstract
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.
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Socorro, J.M., Olmo, R., Teijón, C. et al. Analysis of Aluminum—Yeast Hexokinase Interaction: Modifications on Protein Structure and Functionality. J Protein Chem 19, 199–208 (2000). https://doi.org/10.1023/A:1007055719926
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DOI: https://doi.org/10.1023/A:1007055719926