title: Structure and activity of DmmA, a marine haloalkane dehalogenase.
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-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.
authors: Life Sciences Institute, University of Michigan, 210 Washtenaw Ave., Ann Arbor, MI 48109, USA.
authors: Jennifer J
authors: JJ
authors: Gehret
authors: Liangcai
authors: L
authors: Gu
authors: Todd W
authors: TW
authors: Geders
authors: William Clay
authors: WC
authors: Brown
authors: Lena
authors: L
authors: Gerwick
authors: William H
authors: WH
authors: Gerwick
authors: David H
authors: DH
authors: Sherman
authors: Janet L
authors: JL
authors: Smith
mesh_terms: D000818:Animals; D059001:Aquatic Organisms / Q000737:chemistry / Q000201:enzymology*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D000458:Cyanobacteria / Q000737:chemistry / Q000201:enzymology / Q000378:metabolism; D004789:Enzyme Activation; D006867:Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D008954:Models, Biological; D008958:Models, Molecular; D055503:Protein Multimerization / Q000502:physiology; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D013379:Substrate Specificity
chemical_list: D006867:Hydrolases; C046137:haloalkane dehalogenase