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2 Janelia Publications

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    Looger Lab
    02/20/09 | Cofactor engineering of lactobacillus brevis alcohol dehydrogenase by computational design.
    Ronnie Machielsen , Loren L. Looger , John Raedts , Sjoerd Dijkhuizen , Werner Hummel , Hans‐Georg Hennemann , Thomas Daussmann , John van der Oost
    Engineering in Life Sciences. 2009 Feb 20;9(1):38-44. doi: 10.1002/elsc.200800046

    The R‐specific alcohol dehydrogenase from Lactobacillus brevis (Lb‐ADH) catalyzes the enantioselective reduction of prochiral ketones to the corresponding secondary alcohols. It is stable and has broad substrate specificity. These features make this enzyme an attractive candidate for biotechnological applications. A drawback is its preference for NADP(H) as a cofactor, which is more expensive and labile than NAD(H). Structure‐based computational protein engineering was used to predict mutations to alter the cofactor specificity of Lb‐ADH. Mutations were introduced into Lb‐ADH and tested against the substrate acetophenone, with either NAD(H) or NADP(H) as cofactor. The mutant Arg38Pro showed fourfold increased activity with acetophenone and NAD(H) relative to the wild type. Both Arg38Pro and wild type exhibit a pH optimum of 5.5 with NAD(H) as cofactor, significantly more acidic than with NADP(H). These and related Lb‐ADH mutants may prove useful for the green synthesis of pharmaceutical precursors.

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    Looger Lab
    02/01/09 | A bright and photostable photoconvertible fluorescent protein.
    McKinney SA, Murphy CS, Hazelwood KL, Davidson MW, Looger LL
    Nature Methods. 2009 Feb;6(2):131-3. doi: 10.1038/nmeth.1296

    Photoconvertible fluorescent proteins are potential tools for investigating dynamic processes in living cells and for emerging super-resolution microscopy techniques. Unfortunately, most probes in this class are hampered by oligomerization, small photon budgets or poor photostability. Here we report an EosFP variant that functions well in a broad range of protein fusions for dynamic investigations, exhibits high photostability and preserves the approximately 10-nm localization precision of its parent.

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