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Journal of Bacteriology, November 2000, p. 6268-6271, Vol. 182, No. 21
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Characterization of Alginate Lyase from Pseudomonas syringae pv. syringae

Lori A. Preston,1 T. Y. Wong,1 Carol L. Bender,2,* and Neal L. Schiller1

Division of Biomedical Sciences, University of California, Riverside, California 92521,1 and Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, Oklahoma 740782

Received 5 May 2000/Accepted 14 August 2000

The gene encoding alginate lyase (algL) in Pseudomonas syringae pv. syringae was cloned, sequenced, and overexpressed in Escherichia coli. Alginate lyase activity was optimal when the pH was 7.0 and when assays were conducted at 42°C in the presence of 0.2 M NaCl. In substrate specificity studies, AlgL from P. syringae showed a preference for deacetylated polymannuronic acid. Sequence alignment with other alginate lyases revealed conserved regions within AlgL likely to be important for the structure and/or function of the enzyme. Site-directed mutagenesis of histidine and tryptophan residues at positions 204 and 207, respectively, indicated that these amino acids are critical for lyase activity.

* Corresponding author. Mailing address: 127 Noble Research Center, Oklahoma State University, Stillwater, OK 74078-3032. Phone: (405) 744-9945. Fax: (405) 744-7373. E-mail: cbender{at}okstate.edu.

Journal of Bacteriology, November 2000, p. 6268-6271, Vol. 182, No. 21
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.




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