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Please use this identifier to cite or link to this item: http://dspace.utalca.cl/handle/1950/4903

Title: Relevance of phenylalanine 216 in the affinity of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase for Mn(II)
Authors: Yevenes, A.
Gonzalez-Nilo, F.
Cardemill, E.
Keywords: Phosphoenolpyruvate carboxykinase; manganese binding site; Saccharomyces cerevisiae; theoretical pK a calculations; manganese ligands in protein
Issue Date: 2007
Publisher: Springer Netherlands
Citation: Protein Journal 26(2): 135-141
Abstract: Saccharomyces cerevisiae phosphoenolpyruvate (PEP) carboxykinase catalyzes the reversible formation of oxaloacetate and adenosine triphosphate from PEP, adenosine diphosphate and carbon dioxide, and uses Mn2+ as the activating metal ion. Comparison with the crystalline structure of homologous Escherichia coli PEP carboxykinase [Tari et al. (1997) Nature Struct. Biol. 4, 990–994] shows that Lys213 is one of the ligands to Mn2+ at the enzyme active site. Coordination of Mn2+ to a lysyl residue is not common and suggests a low pK a value for the ε-NH2 group of Lys213. In this work, we evaluate the role of neighboring Phe216 in contributing to provide a low polarity microenvironment suitable to keep the ε-NH2 of Lys213 in the unprotonated form. Mutation Phe216Tyr shows that the introduction of a hydroxyl group in the lateral chain of the residue produces a substantial loss in the enzyme affinity for Mn2+, suggesting an increase of the pK a of Lys213. In agreement with this interpretation, theoretical calculations indicate an alkaline shift of 2.8 pH units in the pK a of the ε-amino group of Lys213 upon Phe216Tyr mutation.
Description: Fernando D. González-Nilo. Centro de Bioinformática y Simulación Molecular, Universidad de Talca, Talca, Chile.
URI: http://dspace.utalca.cl/handle/1950/4903
ISSN: 1572-3887
Appears in Collections:Artículos en publicaciones ISI - Universidad de Talca

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