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J. Bacteriol., 06 1995, 3213-3219, Vol 177, No. 11
EI Kozliak, JA Fuchs, MB Guilloton and PM Anderson
Cyanase is an inducible enzyme in Escherichia coli that catalyzes the
reaction of cyanate with bicarbonate to give two CO2 molecules. The gene
for cyanase is part of the cyn operon, which includes cynT and cynS,
encoding carbonic anhydrase and cyanase, respectively. Carbonic anhydrase
functions to prevent depletion of cellular bicarbonate during cyanate
decomposition (the product CO2 can diffuse out of the cell faster than
noncatalyzed hydration back to bicarbonate). Addition of cyanate to the
culture medium of a delta cynT mutant strain of E. coli (having a
nonfunctional carbonic anhydrase) results in depletion of cellular
bicarbonate, which leads to inhibition of growth and an inability to
catalyze cyanate degradation. These effects can be overcome by aeration
with a higher partial CO2 pressure (M. B. Guilloton, A. F. Lamblin, E. I.
Kozliak, M. Gerami-Nejad, C. Tu, D. Silverman, P. M. Anderson, and J. A.
Fuchs, J. Bacteriol. 175:1443- 1451, 1993). The question considered here is
why depletion of bicarbonate/CO2 due to the action of cyanase on cyanate in
a delta cynT strain has such an inhibitory effect. Growth of wild-type E.
coli in minimal medium under conditions of limited CO2 was severely
inhibited, and this inhibition could be overcome by adding certain Krebs
cycle intermediates, indicating that one consequence of limiting CO2 is
inhibition of carboxylation reactions. However, supplementation of the
growth medium with metabolites whose syntheses are known to depend on a
carboxylation reaction was not effective in overcoming inhibition related
to the bicarbonate deficiency induced in the delta cynT strain by addition
of cyanate.(ABSTRACT TRUNCATED AT 250 WORDS)
Copyright © 1995, American Society for Microbiology
Role of bicarbonate/CO2 in the inhibition of Escherichia coli growth by cyanate
Department of Biochemistry and Molecular Biology, University of Minnesota-Duluth 55812, USA.
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