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  • Title: Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis.
    Author: Hartmann MD, Bourenkov GP, Oberschall A, Strizhov N, Bartunik HD.
    Journal: J Mol Biol; 2006 Dec 01; 364(3):411-23. PubMed ID: 17020768.
    Abstract:
    The structural mechanism of the catalytic functioning of shikimate kinase from Mycobacterium tuberculosis was investigated on the basis of a series of high-resolution crystal structures corresponding to individual steps in the enzymatic reaction. The catalytic turnover of shikimate and ATP into the products shikimate-3-phosphate and ADP, followed by release of ADP, was studied in the crystalline environment. Based on a comparison of the structural states before initiation of the reaction and immediately after the catalytic step, we derived a structural model of the transition state that suggests that phosphoryl transfer proceeds with inversion by an in-line associative mechanism. The random sequential binding of shikimate and nucleotides is associated with domain movements. We identified a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate.
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