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J. Biol. Chem., Vol. 278, Issue 20, 18117-18123, May 16, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/20/18117    most recent M301983200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wu, J. Articles by Woodard, R. W. Search for Related Content PubMed PubMed Citation Articles by Wu, J. Articles by Woodard, R. W. Social Bookmarking                      What's this?

Escherichia coli YrbI Is 3-Deoxy-D-manno-octulosonate 8-Phosphate Phosphatase^*

Jing Wu and Ronald W. Woodard

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 K_m of 75 µM and a k_cat of 175 s¹ 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.

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