FEBS Letters
Volume 583, Issue 13 , Pages 2231-2236, 7 July 2009

Mycobacterial adenosine kinase is not a typical adenosine kinase

Edited by Judit Ovádi

Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Canada L8N 3Z5

Received 13 March 2009; received in revised form 19 May 2009; accepted 2 June 2009. published online 08 June 2009.

Abstract 

Adenosine kinase (AK) is only found in eukaryotes. Recently, a Mycobacterium tuberculosis (MTub) protein exhibiting greater sequence similarity to ribokinases (RK) was identified as AK. We have expressed AKs from MTub, human and Chinese hamster (CH) cells in Escherichia coli and also AK from human and MTub in AK-deficient CH cells. While both E. coli and CH cells expressing mammalian AKs efficiently metabolized various adenosine analogs, those expressing MTub-AK were completely inactive. The AK activity of the MTub protein was very low (50-fold lower than E. coli RK) and it was not stimulated by phosphate or inhibited by several AK inhibitors. These results raise questions over MTub protein’s true function and whether it functions as AK in cells.

Keywords: Adenosine kinase, PfkB family of protein, Ribokinase, Adenosine analog, Mycobacterial adenosine kinase, Adenosine kinase inhibitor, Rv2202c

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PII: S0014-5793(09)00441-4

doi:10.1016/j.febslet.2009.06.002

FEBS Letters
Volume 583, Issue 13 , Pages 2231-2236, 7 July 2009