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
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
https://www.wwpdb.org/pdb?id=pdb_00006xw
Widely applicable background depletion step enables transaminase evolution through solid-phase screening
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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