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Fourier transform ion cyclotron resonance MS reveals the presence of a water molecule in an enzyme transition-state analogue complex

  1. Author:
    Borchers, C. H.
    Marquez, V. E.
    Schroeder, G. K.
    Short, S. A.
    Snider, M. J.
    Speir, J. P.
    Wolfenden, R.

  2. Author Address

    Univ N Carolina, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA. NCI, Ctr Canc Res, Med Chem Lab, Ft Detrick, MD 21702 USA. GlaxoSmithKline, Dept Gene Express & Prot Biochem, Res Triangle Pk, NC 27709 USA. Bruker Dalton, Billerica, MA 01821 USA. Coll Wooster, Dept Chem, Wooster, OH 44691 USA Wolfenden, R, Univ N Carolina, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA
    1. Year: 2004
    2. Date: OCT 26
  2. Journal: Proceedings of the National Academy of Sciences of the United States of America
    1. 101
    2. 43
    3. Pages: 15341-15345
  4. Type of Article: Article
  1. Abstract:

    The structures of several powerful inhibitors of hydrolytic enzymes resemble that of the altered substrate in the transition state, except that a hydrogen atom replaces one substituent (typically the leaving group). To test the hypothesis that a water molecule might be present in the gap resulting from this replacement, we examined a transition-state analogue complex formed by Escherichia coli cytidine deaminase by Fourier transform ion cyclotron resonance MS in electrospray mode. Upon nebularization from aqueous solution under conditions (pH 5.6) where the enzyme is active, cytidine deaminase remains dimeric in the vapor phase. In the presence of inhibitor, the enzyme's exact mass can be used to infer the presence at each active site of zinc, 5-fluoro-3,4-dihydrouridine, and a single water molecule

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External Sources

  1. View record in Web of Science®
  2. WOS: 000224782400014

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