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Reaction trajectory of pyrophosphoryl transfer catalyzed by 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase

  1. Author:
    Blaszczyk, J.
    Shi, G. B.
    Li, Y.
    Yan, H. G.
    Ji, X. H.

  2. Author Address

    Ji, XH, NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA. Michigan State Univ, Dept Biochem, E Lansing, MI 48824 USA. Vanderbilt Univ, Sch Med, Div Nephrol, MCN, Nashville, TN 37232 USA.
    1. Year: 2004
  2. Journal: Structure
    1. 12
    2. 3
    3. Pages: 467-475
  4. Type of Article: Article
  1. Abstract:

    6-hydroxymethyl-7,8-dihydropterin pyrophospholkinase (HPPK) catalyzes the Mg2+-dependent pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP). The reaction follows a bi-bi mechanism with ATP as the first substrate and AMP and HIP pyrophosphate (HPPP) as the two products. HPPK is a key enzyme in the folate biosynthetic pathway and is essential for microorganisms but absent from mammals. For the HPPK-catalyzed pyrophosphoryl transfer, a reaction coordinate is constructed on the basis of the thermodynamic and transient kinetic data we reported previously, and the reaction trajectory is mapped out with five three-dimensional structures of the enzyme at various liganded states. The five structures are apo-HPPK (ligand-free enzyme), HPPK(.)MgATP(analog) (binary complex of HPPK with its first substrate) and HPPK-MgATP(analog) HP (ternary complex of HPPK with both substrates), which we reported previously, and HPPK-AMP-HPPP (ternary complex of HPPK with both product molecules) and HPPK-HPPP (binary complex of HPPK with one product), which we present in this study

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