Curtin University Homepage
  • Library
  • Help
    • Admin

    espace - Curtin’s institutional repository

    JavaScript is disabled for your browser. Some features of this site may not work without it.
    View Item 
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item

    The molecular binding interactions of inhibitors and activators of phosphoenolpyruvate carboxylase

    19744_19744.pdf (654.6Kb)
    Access Status
    Open access
    Authors
    Mancera, Ricardo
    Carrington, B.
    Date
    2005
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Mancera, Ricardo L. and Carrington, Benjamin J. 2005. The molecular binding interactions of inhibitors and activators of phosphoenolpyruvate carboxylase. Journal of Molecular Structure: THEOCHEM. 755 (91-30): 151-159.
    Source Title
    Journal of Molecular Structure: THEOCHEM
    DOI
    10.1016/j.theochem.2005.08.014
    Faculty
    Division of Health Sciences
    School of Pharmacy
    Remarks

    NOTICE: this is the author’s version of a work that was accepted for publication in Journal of Molecular Structure: THEOCHEM. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Molecular Structure: THEOCHEM, Volume 755, Issues 1–3, 30 November 2005, Pages 151–159, http://dx.doi.org/10.1016/j.theochem.2005.08.014

    Copyright 2006 © Elsevier B.V.

    URI
    http://hdl.handle.net/20.500.11937/8995
    Collection
    • Curtin Research Publications
    Abstract

    We have performed molecular modelling studies of the binding to maize phosphoenolpyruvate carboxylase (PEPC) of phosphoenolpyruvate (PEP) and a number of representative competitive inhibitors. We predict that all these compounds share a common binding mode and that the differences in inhibitory activity of the various inhibitors arise mainly from either increased hydrophobic interactions of cis substituents or small but significant changes in their binding mode arising from steric clashes of trans substituents with the active site. We have also performed molecular modelling studies of glucose-6-phosphate (G6P) and a number of other allosteric activators in their putative allosteric binding site in this enzyme. We predict that these molecules share the same binding mode for their phosphate moiety while some of them engage in a variety of hydrogen bonding interactions with residues from different subunits of the enzyme, and others establish hydrophobic and van der Waals interactions with other regions of the allosteric binding site.

    Related items

    Showing items related by title, author, creator and subject.

    • Molecular modelling of the interactions of complex carbohydrates with proteins
      Gandhi, Neha Sureshchandra (2011)
      Glycosaminoglycans (GAGs) are ubiquitous complex carbohydrate molecules present on the cell surfaces and in extracellular matrices (ECM) of vertebrate and invertebrate tissues. The interactions of sulphated GAGs such as ...
    • Molecular Modeling Study for Inhibition Mechanism of Human Chymase and Its Application in Inhibitor Design
      Arooj, Mahreen; Kim, Songmi; Sakkiah, Sugunadevi; Ping Cao, Guang; Lee, Yuno; Woo Lee, Keun (2013)
      Human chymase catalyzes the hydrolysis of peptide bonds. Three chymase inhibitors with very similar chemical structures but highly different inhibitory profiles towards the hydrolase function of chymase were selected with ...
    • Novel Structural Features of CDK Inhibition Revealed by an ab Initio Computational MethodCombined with Dynamic Simulations
      Heady, L.; Fernandez-Serra, M.; Mancera, Ricardo; Joyce, S.; Venkitaraman, A.; Artacho, E.; Skylaris, C.; Ciacchi, L.; Payne, M. (2006)
      The rational development of specific inhibitors for the ~500 protein kinases encoded in the human genome is impeded by a poor understanding of the structural basis for the activity and selectivity of small molecules that ...
    Advanced search

    Browse

    Communities & CollectionsIssue DateAuthorTitleSubjectDocument TypeThis CollectionIssue DateAuthorTitleSubjectDocument Type

    My Account

    Admin

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Follow Curtin

    • 
    • 
    • 
    • 
    • 

    CRICOS Provider Code: 00301JABN: 99 143 842 569TEQSA: PRV12158

    Copyright | Disclaimer | Privacy statement | Accessibility

    Curtin would like to pay respect to the Aboriginal and Torres Strait Islander members of our community by acknowledging the traditional owners of the land on which the Perth campus is located, the Whadjuk people of the Nyungar Nation; and on our Kalgoorlie campus, the Wongutha people of the North-Eastern Goldfields.