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Originally published In Press as doi:10.1074/jbc.M107953200 on February 15, 2002

J. Biol. Chem., Vol. 277, Issue 18, 15573-15578, May 3, 2002
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Isolation of a Glucosamine-specific Kinase, a Unique Enzyme of Vibrio cholerae*

Jae Kweon ParkDagger §, Lai-Xi Wang, and Saul RosemanDagger ||

From the Dagger  Department of Biology and the McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218 and the  Institute of Human Virology, University of Maryland Biotechnology Institute, The University of Maryland, Baltimore, Maryland 21201

We showed previously that chitin catabolism by the marine bacterium Vibrio furnissii involves at least three signal transduction systems and many genes, several of which were molecularly cloned, and the corresponding proteins were characterized. The predicted amino acid sequences of these proteins showed a high degree of identity to the corresponding proteins from Vibrio cholerae, whose complete genomic sequence has recently been determined. We have therefore initiated studies with V. cholerae. We report here a novel ATP-dependent glucosamine kinase of V. cholerae encoded by a gene designated gspK. The protein, GspK (31.6 kDa), was purified to apparent homogeneity from recombinant Escherichia coli. The product of the reaction was shown to be GlcN-6-P by matrix-assisted laser desorption/ionization-time of flight (MALDI mass spectrometry) and NMR. The Km values for GlcN, ATP, and MgCl2 were 0.45, 2.4, and 2.2 mM, respectively, and the Vmax values were in the range 180-200 nmol/µg/min (~6 nmol/pmol/min). Kinase activity was not observed with any other sugar, including: galactosamine, mannosamine, Glc, GlcNAc, GalNAc, mannose, 2-deoxyglucose, and oligosaccharides of chitosan. The enzyme is also ATP-specific. The kinase can be used to specifically determine micro quantities of GlcN in acid hydrolysates of glycoconjugates. The physiological function of this enzyme remains to be determined.

* This work was supported by Grant GM51215 from the National Institutes of Health.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.

§ Present address: ISM Biopolymer, 220 Denison E. Granby, Quebec J2H 2R6, Canada.

|| To whom correspondence should be addressed: Dept. of Biology and the McCollum-Pratt Institute, The Johns Hopkins University, Mudd Hall, Rm. 214, 3400 N. Charles St., Baltimore, MD 21218. Tel.: 410-516-7333; Fax: 410-516-5213.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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