Abstract
Dimethylsulfoniopropionate (DMSP) is degraded to dimethylsulfide (DMS) and acrylate by the enzyme DMSP lyase. DMS or acrylate can serve as a carbon source for both free-living and endophytic bacteria in the marine environment. In this study, we report on the mechanism of DMSP-acrylate metabolism by Alcaligenes faecalis M3A. Suspensions of citrate-grown cells expressed a low level of DMSP lyase activity that could be induced to much higher levels in the presence of DMSP, acrylate, and its metabolic product, beta-hydroxypropionate. DMSP was degraded outside the cell, resulting in an extracellular accumulation of acrylate, which in suspensions of citrate-grown cells was then metabolized at a low endogenous rate. The inducible nature of acrylate metabolism was evidenced by both an increase in the rate of its degradation over time and the ability of acrylate-grown cells to metabolize this molecule at about an eight times higher rate than citrate-grown cells. Therefore, acrylate induces both its production (from DMSP) and its degradation by an acrylase enzyme. (1)H and (13)C nuclear magnetic resonance analyses were used to identify the products resulting from [1-(13)C]acrylate metabolism. The results indicated that A. faecalis first metabolized acrylate to beta-hydroxypropionate outside the cell, which was followed by its intracellular accumulation and subsequent induction of DMSP lyase activity. In summary, the mechanism of DMSP degradation to acrylate and the subsequent degradation of acrylate to beta-hydroxypropionate in the aerobic beta-Proteobacterium A. faecalis has been described.
MeSH Terms
Acrylates/metabolism
Alcaligenes/isolation & purification,metabolism
Biodegradation, Environmental
Carbon-Sulfur Lyases/biosynthesis
Enzyme Induction
Geologic Sediments/microbiology
Kinetics
Sulfonium Compounds/pharmacokinetics
Water Microbiology
Chemicals
Acrylates
Sulfonium Compounds
dimethylpropiothetin
Carbon-Sulfur Lyases
dimethylsulfoniopropionate lyase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ansede J H
Department of Biological Sciences, University of South Carolina, Columbia, South Carolina 29208, USA.
Pellechia P J
Yoch D C
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