Amcr. Alves et al., Different physiological roles of ATP- and PPi-Dependent phosphofructokinase isoenzymes in the methylotrophic actinomycete Amycolatopsis methanolica, J BACT, 183(24), 2001, pp. 7231-7240
Cells of the actinomycete Amycolatopsis methanolica grown on glucose posses
s only a single, exclusively PPi-dependent phosphofructokinase (PPi-PFK) (A
. M. C. R. Alves, G. J. W. Euverink, H. J. Hektor, J. van der Vlag, W. Vrij
bloed, D.H.A. Hondmann, J. Visser, and L. Dijkhuizen, J. Bacteriol. 176:682
7-6835, 1994). When this methylotrophic bacterium is grown on one-carbon (C
-1) compounds (e.g., methanol), an ATP-dependent phosphofructokinase (ATP-P
FK) activity is specifically induced, completely replacing the PPi-PFK. The
two A. methanolica PFK isoenzymes have very distinct functions, namely, in
the metabolism of C-6 and C-1 carbon substrates. This is the first report
providing biochemical evidence for the presence and physiological roles of
PPi-PFK and ATP-PFK isoenzymes in a bacterium. The novel ATP-PFK enzyme was
purified to homogeneity and characterized in detail at the biochemical and
molecular levels. The A. methanolica ATP-PFK and PPi-PFK proteins possess
a low level of amino acid sequence similarity (24%), clearly showing that t
he two proteins are not the result of a gene duplication event. PPi-PFK is
closely related to other (putative) actinomycete PFK enzymes. Surprisingly,
the A. methanolica ATP-PFK is most similar to ATP-PFK from the protozoon T
rypanosoma brucei and PPi-PFK proteins from the bacteria Borrelia burgdorfe
ri and Treponema pallidum, both spirochetes, very distinct from actinomycet
es. The data thus suggest that A. methanolica obtained the ATP-PFK-encoding
gene via a lateral gene transfer event.