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J. Biol. Chem., Vol. 276, Issue 40, 37415-37425, October 5, 2001

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Metabolism of Sucrose and Its Five Linkage-isomeric -D-Glucosyl-D-fructoses by Klebsiella pneumoniae
PARTICIPATION AND PROPERTIES OF SUCROSE-6-PHOSPHATE HYDROLASE AND PHOSPHO--GLUCOSIDASE^*

John Thompson^§, Stanley A. Robrish, Stefan Immel^¶, Frieder W. Lichtenthaler^¶, Barry G. Hall, and Andreas Pikis^**

From the  Microbial Biochemistry and Genetics Unit, Oral Infection and Immunity Branch, NIDCR, National Institutes of Health, Bethesda, Maryland 20892, the ^¶ Institut für Organische Chemie, Technische Universität Darmstadt, D-64287 Darmstadt, Germany, the  Biology Department, University of Rochester, Rochester, New York 14627-0211, the ^** Vaccine and Therapeutic Development Section, Oral and Infection and Immunity Branch, NIDCR, National Institutes of Health, Bethesda, Maryland 20892, and the  Department of Infectious Diseases, Children's National Medical Center, Washington, D. C. 20010-2970

Klebsiella pneumoniae is presently unique among bacterial species in its ability to metabolize not only sucrose but also its five linkage-isomeric -D-glucosyl-D-fructoses: trehalulose, turanose, maltulose, leucrose, and palatinose. Growth on the isomeric compounds induced a protein of molecular mass ~ 50 kDa that was not present in sucrose-grown cells and which we have identified as an NAD⁺ and metal ion-dependent 6-phospho--glucosidase (AglB). The aglB gene has been cloned and sequenced, and AglB (M_r = 49,256) has been purified from a high expression system using the chromogenic p-nitrophenyl -glucopyranoside 6-phosphate as substrate. Phospho--glucosidase catalyzed the hydrolysis of a wide variety of 6-phospho--glucosides including maltose-6'-phosphate, maltitol-6-phosphate, isomaltose-6'-phosphate, and all five 6'-phosphorylated isomers of sucrose (K_m ~ 1-5 mM) yet did not hydrolyze sucrose-6-phosphate. By contrast, purified sucrose-6-phosphate hydrolase (M_r ~ 53,000) hydrolyzed only sucrose-6-phosphate (K_m ~ 80 µM). Differences in molecular shape and lipophilicity potential between sucrose and its isomers may be important determinants for substrate discrimination by the two phosphoglucosyl hydrolases. Phospho--glucosidase and sucrose-6-phosphate hydrolase exhibit no significant homology, and by sequence-based alignment, the two enzymes are assigned to Families 4 and 32, respectively, of the glycosyl hydrolase superfamily. The phospho--glucosidase gene (aglB) lies adjacent to a second gene (aglA), which encodes an EII(CB) component of the phosphoenolpyruvate-dependent sugar:phosphotransferase system. We suggest that the products of the two genes facilitate the phosphorylative translocation and subsequent hydrolysis of the five -D-glucosyl-D-fructoses by K. pneumoniae.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AF337811.

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