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A more recent version of this article appeared on October 13, 2000
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Papers In Press, published online ahead of print July 25, 2000
J. Biol. Chem, 10.1074/jbc.M001042200
Submitted on February 8, 2000
Revised on May 25, 2000
Accepted on July 25, 2000

Chitin Catabolism in the Marine Bacterium Vibrio furnissii: Identification, Molecular Cloning, and Characterization of an N,N'-Diacetylchitobiose phosphorylase

Jae K. Park, Nemat O. Keyhani, and Saul Roseman

Department of Biology, Johns Hopkins University, Baltimore, MD 21218

Corresponding Author: roseman{at}jhu.edu

The major product of bacterial chitinases is N,N'-diacetylchitobiose, or (GlcNAc)2. We have previously demonstrated that (GlcNAc)2 is taken up unchanged by a specific permease in V. furnissii (unlike Escherichia coli). It is generally held that marine Vibrios further metabolize cytoplasmic (GlcNAc)2 by hydrolyzing it to 2 GlcNAc (i.e., a ?chitobiase ?). Here we report instead that V. furnissii expresses a novel phosphorylase. The gene, chbP, was cloned into Escherichia coli; the enzyme, ChbP, was purified to apparent homogeneity, and characterized kinetically. The DNA sequence indicates that chbP encodes an 89 kDa protein. The enzymatic reaction was characterized as follows: (GlcNAc)2 + Pi {double direction arrows} GlcNAc-alpha -1-P + GlcNAc K?eq = 1.0 ± 0.2. The Km values for the 4 substrates were in the range 0.3-1 mM. p-Nitrophenyl-beta -(GlcNAc)2 was cleaved at 8.5% the rate of (GlcNAc)2, and PNP-GlcNAc was 36% as active as GlcNAc in the reverse direction. All other compounds tested displayed =1% of the activity of the indicated substrates including: phosphorolysis, higher chitin oliogsaccharides, (GlcNAc)n, n = 3-5; cellobiose; PNP-GlcNAc, and PNP-(GlcNAc)3; synthesis, (GlcNAc)n, n = 2-5; glucose, etc. (GlcNAc)2 is a major regulator of the chitin catabolic cascade. Conceivably GlcNAc-alpha -1-P plays a similar, but different role in regulation.


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