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J. Biol. Chem., Vol. 278, Issue 20, 18117-18123, May 16, 2003
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From the Department of Medicinal Chemistry and Department of
Chemistry, University of Michigan,
Ann Arbor, Michigan 48109-1065
3-Deoxy-D-manno-octulosonate
8-phosphate (KDO 8-P) phosphatase, which catalyzes the hydrolysis of
KDO 8-P to KDO and inorganic phosphate, is the last enzyme in the KDO
biosynthetic pathway for which the gene has not been identified.
Wild-type KDO 8-P phosphatase was purified from Escherichia
coli B, and the N-terminal amino acid sequence matched a
hypothetical protein encoded by the E. coli open reading
frame, yrbI. The yrbI gene, which encodes for a
protein of 188 amino acids, was cloned, and the gene product was
overexpressed in E. coli. The recombinant enzyme is a
tetramer and requires a divalent metal cofactor for activity. Optimal
enzymatic activity is observed at pH 5.5. The enzyme is highly specific for KDO 8-P with an apparent Km of 75 µM and a kcat of 175 s
Escherichia coli YrbI Is
3-Deoxy-D-manno-octulosonate 8-Phosphate
Phosphatase*
1 in the presence of 1 mM Mg2+.
Amino acid sequence analysis indicates that KDO 8-P phosphatase is a
member of the haloacid dehalogenase hydrolase superfamily.
*
This work was supported by National Institutes of
Health Grant GM 53069 (to R. W. W.).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: College of
Pharmacy, 428 Church St., Ann Arbor, MI 48109-1065. Tel.:
734-764-7366; Fax: 734-763-2022; E-mail: rww@umich.edu.
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