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Applied and Environmental Microbiology, November 1999, p. 5075-5081, Vol. 65, No. 11
Department of Biological
Sciences1 and Department of Chemistry
and Biochemistry,2 University of South Carolina,
Columbia, South Carolina 29208
Received 2 July 1999/Accepted 31 August 1999
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,
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Metabolism of Acrylate to
-Hydroxypropionate and
Its Role in Dimethylsulfoniopropionate Lyase Induction by a Salt Marsh
Sediment Bacterium, Alcaligenes faecalis M3A
-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. 1H
and 13C nuclear magnetic resonance analyses were used to
identify the products resulting from [1-13C]acrylate
metabolism. The results indicated that A. faecalis first
metabolized acrylate to -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
-hydroxypropionate in the aerobic -Proteobacterium A. faecalis has been described.
*
Corresponding author. Mailing address: Department of
Biological Sciences, University of South Carolina, Columbia, SC 29208. Phone: (803) 777-2322. Fax: (803) 777-4002. E-mail:
yoch{at}biol.sc.edu.
Applied and Environmental Microbiology, November 1999, p. 5075-5081, Vol. 65, No. 11
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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