A new subfamily of short bacterial adenylate kinases with the Mycobacteriumtuberculosis enzyme as a model: A predictive and experimental study
✍ Scribed by Hélène Munier-Lehmann; Simona Burlacu-Miron; Constantin T. Craescu; Henry H. Mantsch; Christian P. Schultz
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 389 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0887-3585
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✦ Synopsis
The adk gene from Mycobacterium tuberculosis codes for an enzyme of 181 amino acids. A sequence comparison with 52 different forms of adenylate kinases (AK) suggests that the enzyme from M. tuberculosis belongs to a new subfamily of ''short'' bacterial AKs. The recombinant protein, overexpressed in Escherichia coli, exhibits a low catalytic activity and an unexpectedly high thermal stability (Tm ؍ 64.8°C). Based on various spectroscopic data, on the known three-dimensional structure of the AK from E. coli and on secondary structure predictions for various sequenced AKs, we propose a structural model for AK from M. tuberculosis (AKmt).