Structure and activity of DmmA, a marine haloalkane dehalogenase
Structure and activity of DmmA, a marine haloalkane dehalogenase
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DOI：
10.1002/pro.2009
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发表时间：
2012-02-01
期刊：
影响因子：
8
通讯作者：
Smith, Janet L.
中科院分区：
文献类型：
--
作者：
Gehret, Jennifer J.;Gu, Liangcai;Smith, Janet L.
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-angstrom 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.
