Open AccessPurification and characterization of a dimethylsulfoniopropionate cleaving enzyme from Desulfovibrio acrylicus
Author(s) -
Der Maarel Marc J.E.C.,
Aukema Walter,
Hansen Theo A.
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08487.x
Subject(s) - dimethylsulfoniopropionate , chemistry , desulfovibrio , chromatography , enzyme , biochemistry , psychrophile , organic chemistry , sulfate , phytoplankton , nutrient
An enzyme that cleaves the algal osmolyte dimethylsulfoniopropionate to dimethylsulfide and acrylate was purified almost 400‐fold from the marine sulfate‐ and acrylate‐reducing bacterium Desulfovibrio acrylicus DSM 10141. Dimethylsulfoniopropionate lyase activity was induced by acrylate and dimethylsulfoniopropionate. At 30 °C, the enzyme had a K m for dimethylsulfoniopropionate of 0.45 mM and a V max of 2590 μmol min −1 mg protein −1 . Dimethylsulfoniopropionate was the only substrate of the enzyme. Among the compounds tested, dimethylsulfoniobutyrate was the most potent inhibitor ( kK i = 0.25 mM). On a denaturing polyacrylamide gel, the protein migrated as a single band of 49 kDa.