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Mycobacterial adenosine kinase is not a typical adenosine kinase
Author(s) -
Park Jae,
Singh Bhag,
Gupta Radhey S.
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.06.002
Subject(s) - adenosine kinase , adenosine , chinese hamster , escherichia coli , protein kinase a , kinase , microbiology and biotechnology , biochemistry , chemistry , biology , in vitro , adenosine deaminase , gene
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.