| Title : Structure and activity of DmmA, a marine haloalkane dehalogenase - Gehret_2012_Protein.Sci_21_239 |
| Author(s) : Gehret JJ , Gu L , Geders TW , Brown WC , Gerwick L , Gerwick WH , Sherman DH , Smith JL |
| Ref : Protein Science , 21 :239 , 2012 |
|
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 (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. |
| PubMedSearch : Gehret_2012_Protein.Sci_21_239 |
| PubMedID: 22124946 |
| Gene_locus related to this paper: 9cyan-q6dnd9 |
| Substrate | 1,3-dibromopropane |
| Gene_locus | 9cyan-q6dnd9 |
| Family | Haloalkane_dehalogenase-HLD2 |
| Structure | 3U1T |
Gehret JJ, Gu L, Geders TW, Brown WC, Gerwick L, Gerwick WH, Sherman DH, Smith JL (2012)
Structure and activity of DmmA, a marine haloalkane dehalogenase
Protein Science
21 :239
Gehret JJ, Gu L, Geders TW, Brown WC, Gerwick L, Gerwick WH, Sherman DH, Smith JL (2012)
Protein Science
21 :239