118,068 research outputs found

    The crystal structure of a highly thermostable carboxyl esterase from Bacillus coagulans

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    The crystal structure of a new transaminase from the marine bacterium Virgibacillus

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    La taureau sacré de Chedenou

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    Gourlay Y. J. L. La taureau sacré de Chedenou. In: École pratique des hautes études, Section des sciences religieuses. Annuaire. Tome 86, 1977-1978. 1977. pp. 467-469

    The crystal structure of Halomonas elongata amino-transferase

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    The crystal structure of secreted antigen BPSL2520

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    The crystal structure of Burkholderia pseudomallei antigen and type I fimbria protein BPSL1626

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    The structure of Trehalose-6-phosphatase from Burkholderia pseudomallei

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    The crystal structure of a highly thermostable carboxyl esterase from Bacillus coagulans in complex with glycerol

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    Crystal structure of an R-selective transaminase from Thermomyces stellatus

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    https://www.wwpdb.org/pdb?id=pdb_00006xw

    Widely applicable background depletion step enables transaminase evolution through solid-phase screening

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    Directed evolution of transaminases is a widespread technique in the development of highly sought-after biocatalysts for industrial applications. This process, however, is challenged by the limited availability of effective high-throughput protocols to evaluate mutant libraries. Here we report a rapid, reliable, and widely applicable background depletion method for solid-phase screening of transaminase variants, which was successfully applied to a transaminase from Halomonas elongata (HEWT), evolved through rounds of random mutagenesis towards a series of diverse prochiral ketones. This approach enabled the identification of transaminase variants in viable cells with significantly improved activity towards parasubstituted acetophenones (up to 60-fold), as well as tetrahydrothiophen-3-one and related substrates. Rationalisation of the mutants was assisted by determination of the high-resolution wild-type HEWT crystal structure presented herein
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