3U1T

Haloalkane Dehalogenase, DmmA, of marine microbial origin

Summary for 3U1T

• Entry DOI: 10.2210/pdb3u1t/pdb
• Descriptor: DmmA Haloalkane Dehalogenase, CHLORIDE ION, MALONATE ION, ... (4 entities in total)
• Functional Keywords: alpha/beta-hydrolase, haloalkane dehalogenase, hydrolase
• Biological source: unidentified
• Total number of polymer chains: 2
• Total formula weight: 69777.24

Authors

Gehret, J.J.,Smith, J.L. (deposition date: 2011-09-30, release date: 2011-12-28, Last modification date: 2024-11-27)

Primary citation

Gehret, J.J.,Gu, L.,Geders, T.W.,Brown, W.C.,Gerwick, L.,Gerwick, W.H.,Sherman, D.H.,Smith, J.L.
Structure and activity of DmmA, a marine haloalkane dehalogenase.
Protein Sci., 21:239-248, 2012

PubMed 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.

PubMed: 22124946
DOI: 10.1002/pro.2009

Experimental method

X-RAY DIFFRACTION (2.2 Å)