Characterization of the two tryptophan residues of the lactose repressor from Escherichia coli by phosphorescence and optical detection of magnetic resonance

Biochemistry ◽  
1993 ◽  
Vol 32 (47) ◽  
pp. 12821-12829 ◽  
Author(s):  
Laura E. Burns ◽  
August H. Maki ◽  
Ronit Spotts ◽  
Kathleen S. Matthews
Keyword(s):  
Escherichia Coli ◽  
Magnetic Resonance ◽  
Optical Detection ◽  
Lactose Repressor ◽  
Tryptophan Residues

scholarly journals Discrimination of Escherichia coli and Shigella spp. by Nuclear Magnetic Resonance Based Metabolomic Characterization of Culture Media

2019 ◽  
Vol 5 (11) ◽  
pp. 1879-1886 ◽  
Author(s):  
Gilles J. P. Rautureau ◽  
Tony L. Palama ◽  
Isabelle Canard ◽  
Caroline Mirande ◽  
Sonia Chatellier ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Culture Media ◽  
Shigella Spp ◽  
Nuclear Magnetic

scholarly journals Characterization of Alginate Lyase from Pseudomonas syringae pv. syringae

2000 ◽  
Vol 182 (21) ◽  
pp. 6268-6271 ◽  
Author(s):  
Lori A. Preston ◽  
T. Y. Wong ◽  
Carol L. Bender ◽  
Neal L. Schiller
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Syringae ◽  
Alginate Lyase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Gene Encoding ◽  
Tryptophan Residues ◽  
Lyase Activity ◽  
Alginate Lyases

ABSTRACT The gene encoding alginate lyase (algL) inPseudomonas 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.

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