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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 J+Biol+Chem
2016 ; 291
(17
): 8987-99
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Evidence That Does Not Support Pyruvate Kinase M2 (PKM2)-catalyzed Reaction as a
Rate-limiting Step in Cancer Cell Glycolysis
#MMPMID26917721
Xie J
; Dai C
; Hu X
J Biol Chem
2016[Apr]; 291
(17
): 8987-99
PMID26917721
show ga
It has been recognized that the rate-limiting function of pyruvate kinase M2
(PKM2) in glycolysis plays an important role in distributing glycolytic
intermediates for anabolic and catabolic purposes in cancer cells. However, after
analysis of the catalytic capacity of PKM2 relative to other glycolytic enzymes,
the regulation range of PKM2 activity, metabolic flux control, and
thermodynamics, we suggest that the PKM2-catalyzed reaction is not a
rate-limiting step in cancer cell glycolysis. Hexokinase and phosphofructokinase
1 (PFK1), the first and third enzyme along the pathway, are rate-limiting enzymes
that limit the overall glycolytic rate, whereas PKM2 and lactate dehydrogenase,
the last two enzymes in the pathway, are for the fast removal of upstream
intermediates to prevent the obstruction of the pathway. The argument is in
accordance with the catalytic capacity of glycolytic enzymes, regulation range of
enzyme activities, metabolic flux control, and thermodynamics.