Structure and activity of DmmA, a marine haloalkane dehalogenase |
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Authors: | Gehret Jennifer J Gu Liangcai Geders Todd W Brown William Clay Gerwick Lena Gerwick William H Sherman David H Smith Janet L |
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Affiliation: | Life Sciences Institute, University of Michigan, 210 Washtenaw Ave., Ann Arbor, MI 48109, USA. |
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Abstract: | DmmA is a haloalkane dehalogenase (HLD) identified and characterized from the metagenomic DNA of a marine microbial consortium. Dehalogenase activity was detected with 1,3-dibromopropane as substrate, with steady-state kinetic parameters typical of HLDs (Km = 0.24 ± 0.05 mM, kcat = 2.4 ± 0.1 s−1). The 2.2-Å crystal structure of DmmA revealed a fold and active site similar to other HLDs, but with a substantially larger active site binding pocket, suggestive of an ability to act on bulky substrates. This enhanced cavity was shown to accept a range of linear and cyclic substrates, suggesting that DmmA will contribute to the expanding industrial applications of HLDs. |
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Keywords: | haloalkane dehalogenase marine microbial consortium α/β hydrolase CurN DmmA |
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