Kirkwood, Mark, Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061, Todd, Jonathan D. and Johnston, Andrew W. B. (2010) The ddP gene of Roseovarius nubinhibens encodes a novel lyase that cleaves dimethylsulfoniopropionate into acrylate plus dimethyl sulfide. Microbiology, 156 (6). pp. 1900-1906. ISSN 1465-2080
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The cloned dddP gene of the marine bacterium Roseovarius nubinhibens allows Escherichia coli to form the volatile dimethyl sulfide (DMS) from dimethylsulfoniopropionate (DMSP), an abundant anti-stress compatible solute made by many marine plankton and macroalgae. Using purified DddP, we show here that this enzyme is a DMSP lyase that cleaves DMSP to DMS plus acrylate. DddP forms a functional homodimeric enzyme, has a pH optimum of 6.0 and was a K m of ∼14 mM for the DMSP substrate. DddP belongs to the M24B family of peptidases, some members of which have metal cofactors. However, the metal chelators EDTA and bipyridyl did not affect DddP activity in vitro and the as-isolated enzyme did not contain metal ions. Thus, DddP resembles those members of the M24B family, such as creatinase, which also act on a non-peptide substrate and have no metal cofactor. Site-directed mutagenesis of the active-site region of DddP completely abolished its activity. Another enzyme, termed DddL, which occurs in other alphaproteobacteria, had also been shown to generate DMS plus acrylate from DMSP. However, DddL and DddP have no sequence similarity to each other, so DddP represents a second, wholly different class of DMSP lyase.
Item Type: | Article |
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Faculty \ School: | Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemistry (former - to 2024) |
UEA Research Groups: | Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Centre for Ocean and Atmospheric Sciences Faculty of Science > Research Groups > Molecular Microbiology |
Depositing User: | Users 2731 not found. |
Date Deposited: | 21 Mar 2012 22:28 |
Last Modified: | 24 Sep 2024 09:13 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/38439 |
DOI: | 10.1099/mic.0.038927-0 |
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