A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity

Authors

Buryska, T., Babkova, P., Vavra, O., Damborsky, J., Prokop, Z.

Source

APPLIED AND ENVIRONMENTAL MICROBIOLOGY 84: e01684-17 (2018)

Abstract

The haloalkane dehalogenase enzyme DmmA was identified by marine metagenomic screening. Determination of its crystal structure revealed an unusually large active site compared to previously characterized haloalkane dehalogenases. Here we present a biochemical characterization of this interesting enzyme with emphasis on its structure-function relationships. DmmA exhibited an exceptionally broad substrate specificity and degraded several halogenated environmental pollutants that are resistant to other members of this enzyme family. In addition to this unique substrate specificity, the enzyme was highly tolerant to organic co-solvents such as dimethyl sulfoxide, methanol, and acetone. Its broad substrate specificity, high over-expression yield (200 mg of protein per litre of cultivation medium; 50% of total protein), good tolerance to organic co-solvents and a broad range of pH make DmmA an attractive biocatalyst for various biotechnological applications.

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Citation

Buryska, T., Babkova, P., Vavra, O., Damborsky, J., Prokop, Z., 2018: A Haloalkane Dehalogenase From a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity. Applied and Environmental Microbiology 84: e01684-17.

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