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Journal of Bacteriology, September 1998, p. 4711-4717, Vol. 180, No. 17
Department of Oral Biology, Dental School,
University of Newcastle upon Tyne, Newcastle upon Tyne, United
Kingdom
Received 13 April 1998/Accepted 17 June 1998
Sequencing upstream of the Streptococcus mutans gene
for a CcpA gene homolog, regM, revealed an open
reading frame, named amy, with homology to genes
encoding
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Intracellular
-Amylase of
Streptococcus mutans
-amylases. The deduced amino acid sequence showed a strong
similarity (60% amino acid identity) to the intracellular
-amylase
of Streptococcus bovis and, in common with
this enzyme, lacked a signal sequence. Amylase activity was found only
in S. mutans cell extracts, with no activity detected in
culture supernatants. Inactivation of amy by insertion of
an antibiotic resistance marker confirmed that S. mutans
has a single
-amylase activity. The amylase activity was induced by
maltose but not by starch, and no acid was produced from starch.
S. mutans can, however, transport limit dextrins and
maltooligosaccharides generated by salivary amylase, but
inactivation of amy did not affect growth on these
substrates or acid production. The amylase digested the glycogen-like
intracellular polysaccharide (IPS) purified from S. mutans,
but the amy mutant was able to digest and produce acid from
IPS; thus, amylase does not appear to be essential for
IPS breakdown. However, when grown on excess maltose, the
amy mutant produced nearly threefold the amount of IPS
produced by the parent strain. The role of Amy has not been
established, but Amy appears to be important in the accumulation of IPS
in S. mutans grown on maltose.
*
Corresponding author. Mailing address: Department of
Oral Biology, Dental School, University of Newcastle upon Tyne,
Newcastle upon Tyne NE2 4BW, United Kingdom. Phone: 44 191 222 7859. Fax: 44 191 222 6137. E-mail: r.r.russell{at}ncl.ac.uk.
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