Structural and physico-chemical characteristics of IBordetella pertussis adenylate kinase, a tryptophan-containing enzyme

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DOIResolve DOI: http://doi.org/10.1111/j.1432-1033.1993.tb18448.x
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TypeArticle
Journal titleEuropean Journal of Biochemistry
ISSN1742-4658
Volume218
Issue3
Pages921927; # of pages: 7
AbstractThe adk gene from the Gram-negative pathogen Bordetella pertussis was cloned by complementing the thermosensitive Escherichia coli adk strain CR341T28. B. pertussis adenylate kinase is a 218-amino-acid protein that has high similarity with adenylate kinase from Escherichia coli and Hemophilus influenzae (57%). A distinct characteristic of enzyme from B. pertussis, not found in other bacterial adenylate kinases, is the presence of a tryptophan residue at position 185. Although distant from the catalytic site, this single tryptophan serves as a convenient probe for monitoring the binding of nucleotide substrates or analogs to the enzyme. Differential scanning calorimetry and equilibrium unfolding experiments in guanidine · HCl indicate similar stabilities for adenylate kinase from B. pertussis and E. coli. An extensive comparison between physico-chemical properties of adenylate kinase from B. pertussis and the enzyme from E. coli showed that the kinetic and structural properties of the two enzymes are very similar. However, infrared spectroscopy has allowed to identify small but significant differences in the secondary structure of the two proteins.
Publication date
PublisherJohn Wiley & Sons, Inc.
LanguageEnglish
AffiliationNRC Institute for Biodiagnostics; National Research Council Canada; NRC Institute for Biological Sciences
Peer reviewedYes
NRC number28
NPARC number9148261
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Record identifier277be912-a4ad-488d-8086-738a060be2d7
Record created2009-06-25
Record modified2017-03-23
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