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A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study.

Abstract : 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 degrees 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). Proteins 1999;36:238-248.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-00167076
Contributor : Hélène Munier-Lehmann <>
Submitted on : Tuesday, August 14, 2007 - 3:18:10 PM
Last modification on : Tuesday, July 21, 2020 - 3:58:58 AM

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  • HAL Id : pasteur-00167076, version 1
  • PUBMED : 10398370

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Hélène Munier-Lehmann, Simona Burlacu-Miron, Constantin Craescu, Henry H. Mantsch, C. P. Schultz. A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study.. Proteins - Structure, Function and Bioinformatics, Wiley, 1999, 36 (2), pp.238-48. ⟨pasteur-00167076⟩

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