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

Hélène Munier-Lehmann (1) , Simona Burlacu-Miron (2) , Constantin T. Craescu (2) , Henry H. Mantsch (3) , C. P. Schultz (3)

1 CSM - Chimie Structurale des Macromolécules
2 Biophysique moléculaire
3 Institute for Biodiagnostics

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.

Hélène Munier-Lehmann, Simona Burlacu-Miron, Constantin T. 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, 1999, 36 (2), pp.238-48. ⟨pasteur-00167076⟩