Structural highlights
Publication Abstract from PubMed
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 (K(m) =0.24+/-0.05 mM, k(cat) =2.4+/-0.1 s-1). The 2.2-A 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.
Structure and activity of DmmA, a marine haloalkane dehalogenase.,Gehret JJ, Gu L, Geders TW, Brown WC, Gerwick L, Gerwick WH, Sherman DH, Smith JL Protein Sci. 2011 Nov 28. doi: 10.1002/pro.2009. PMID:22124946[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gehret JJ, Gu L, Geders TW, Brown WC, Gerwick L, Gerwick WH, Sherman DH, Smith JL. Structure and activity of DmmA, a marine haloalkane dehalogenase. Protein Sci. 2011 Nov 28. doi: 10.1002/pro.2009. PMID:22124946 doi:10.1002/pro.2009
