Characterization of Alginate Lyase from Pseudomonas syringae pv. syringae-Reference-Cited by-同舟云学术

Characterization of Alginate Lyase from Pseudomonas syringae pv. syringae

Published:2000-11 Issue:21 Volume:182 Page:6268-6271
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Preston Lori A.¹,Wong T. Y.¹,Bender Carol L.²,Schiller Neal L.¹

Affiliation:

1. Division of Biomedical Sciences, University of California, Riverside, California 92521,1and

2. Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, Oklahoma 740782

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.182.21.6268-6271.2000

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