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J. Biol. Chem., Vol. 277, Issue 24, 21567-21575, June 14, 2002
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From the Escherichia coli strain K4 produces
the K4 antigen, a capsule polysaccharide consisting of a chondroitin
backbone (GlcUA The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number(s) AB079602.
Molecular Cloning and Characterization of Chondroitin Polymerase
from Escherichia coli Strain K4*
§,§,, and
Institute for Molecular Science of Medicine,
Aichi Medical University, Yazako, Nagakute, Aichi 480-1195, § Central Research Laboratories, Seikagaku Corporation,
Tateno, Higashiyamato-shi, Tokyo 207-0021, and ¶ Department of
Chemistry, Graduate School of Science, Hokkaido University, Kita-ku,
Sapporo 060-0810, Japan
(1-3)-GalNAc (1-4))n to which
-fructose is linked at position C-3 of the GlcUA residue. We
molecularly cloned region 2 of the K4 capsular gene cluster essential
for biosynthesis of the polysaccharide, and we further identified a
gene encoding a bifunctional glycosyltransferase that polymerizes the
chondroitin backbone. The enzyme, containing two conserved
glycosyltransferase sites, showed 59 and 61% identity at the amino
acid level to class 2 hyaluronan synthase and chondroitin synthase from
Pasteurella multocida, respectively. The soluble enzyme
expressed in a bacterial expression system transferred GalNAc and GlcUA
residues alternately, and polymerized the chondroitin chain up to a
molecular mass of 20 kDa when chondroitin sulfate hexasaccharide was
used as an acceptor. The enzyme exhibited apparent Km values for UDP-GlcUA and UDP-GalNAc of 3.44 and
31.6 µM, respectively, and absolutely required acceptors
of chondroitin sulfate polymers and oligosaccharides at least longer
than a tetrasaccharide. In addition, chondroitin polymers and
oligosaccharides and hyaluronan polymers and oligosaccharides served as
acceptors for chondroitin polymerization, but dermatan sulfate and
heparin did not. These results may lead to elucidation of the mechanism
for chondroitin chain synthesis in both microorganisms and mammals.
*
This work was supported by a preparatory grant for research
at the Division of Matrix Glycoconjugates, Research Center for Infectious Disease, Aichi Medical University, by a grant-in-aid from
the Ministry of Education, Science, Sports, and Culture of Japan, and
by a special research fund from Seikagaku Corp.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Institute for
Molecular Science of Medicine, Aichi Medical University, Yazako, Nagakute, Aichi 480-1195, Japan. Tel.: 81-52-264-4811 (ext. 2087); Fax:
81-561-63-3532; E-mail: kimata@aichi-med-u.ac.jp.
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