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Papers In Press, published online ahead of print February 15, 2002
Department of Biology, Johns Hopkins University, Baltimore, MD 21218
Corresponding Author: roseman{at}jhu.edu
In earlier work, we showed that the catabolism of chitin by the marine bacterium Vibrio furnissii involves at least three signal transduction systems and many genes. Several genes were molecularly cloned and the corresponding proteins characterized. The predicted amino acid sequences of many of these proteins showed a high degree of identity to the corresponding proteins from V. cholerae, whose complete genomic sequence has recently been determined. We have therefore initiated studies on chitin catabolism by V. cholerae. We report here a novel ATP dependent glucosamine kinase of V. cholerae encoded by a gene designated gspK. The protein, GspK (30 kDa), was purified to apparent homogeneity from recombinant Escherichia coli. The product of the reaction was shown to be GlcN-6-P by MALDI 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/mg/min. Kinase activity was not observed with any other sugar, including:galactosamine, mannosamine, Glc, GlcNAc, GalNAc, mannose, 2-deoxyglucose, and the di- and trisaccharides of chitosan. Little to no activity was detected with nucleoside triphosphates other than ATP. The physiological function of this enzyme remains to be determined.
J. Biol. Chem, 10.1074/jbc.M107953200
Submitted on August 17, 2001
Revised on February 7, 2002
Accepted on February 15, 2002
Isolation of a glucosamine specific kinase, a unique enzyme of Vibrio cholerae
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