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Structure and activity of DmmA, a marine haloalkane dehalogenase
dc.contributor.authorGehret, Jennifer J.en_US
dc.contributor.authorGu, Liangcaien_US
dc.contributor.authorGeders, Todd W.en_US
dc.contributor.authorBrown, William Clayen_US
dc.contributor.authorGerwick, Lenaen_US
dc.contributor.authorGerwick, William H.en_US
dc.contributor.authorSherman, David H.en_US
dc.contributor.authorSmith, Janet L.en_US
dc.date.accessioned2012-03-16T15:57:39Z
dc.date.available2013-04-01T14:17:23Zen_US
dc.date.issued2012-02en_US
dc.identifier.citationGehret, Jennifer J.; Gu, Liangcai; Geders, Todd W.; Brown, William Clay; Gerwick, Lena; Gerwick, William H.; Sherman, David H.; Smith, Janet L. (2012). "Structure and activity of DmmA, a marine haloalkane dehalogenase." Protein Science 21(2): 239-248. <http://hdl.handle.net/2027.42/90241>en_US
dc.identifier.issn0961-8368en_US
dc.identifier.issn1469-896Xen_US
dc.identifier.urihttps://hdl.handle.net/2027.42/90241
dc.description.abstractDmmA 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. PDB Code(s): 3U1Ten_US
dc.publisherWiley Subscription Services, Inc., A Wiley Companyen_US
dc.subject.otherHaloalkane Dehalogenaseen_US
dc.subject.otherMarine Microbial Consortiumen_US
dc.subject.otherα/β Hydrolaseen_US
dc.subject.otherCurNen_US
dc.subject.otherDmmAen_US
dc.titleStructure and activity of DmmA, a marine haloalkane dehalogenaseen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, MIen_US
dc.contributor.affiliationumLife Sciences Institute, University of Michigan, Ann Arbor, MIen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MIen_US
dc.contributor.affiliationumDepartment of Medicinal Chemistry, University of Michigan, Ann Arbor, MIen_US
dc.contributor.affiliationumCenter for Structural Biology, University of Michigan, Ann Arbor, MI 48109en_US
dc.contributor.affiliationumLife Sciences Institute, University of Michigan, 210 Washtenaw Ave., Ann Arbor, MI 48109en_US
dc.contributor.affiliationumDepartment of Microbiology and Immunology, University of Michigan, Ann Arbor, MIen_US
dc.contributor.affiliationotherCenter for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California at San Diego, La Jolla, CA 92093en_US
dc.contributor.affiliationotherR&D Systems, Inc., Minneapolis, MNen_US
dc.contributor.affiliationotherDepartment of Genetics, Harvard Medical School, 77 Ave Louis Pasteur, NRB 232, Boston, MA 02115en_US
dc.contributor.affiliationotherSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, La Jolla, California 92093en_US
dc.identifier.pmid22124946en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/90241/1/PRO_2009_sm_suppinfo.pdf
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/90241/2/2009_ftp.pdf
dc.identifier.doi10.1002/pro.2009en_US
dc.identifier.sourceProtein Scienceen_US
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dc.owningcollnameInterdisciplinary and Peer-Reviewed


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