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findings showed glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells
Phosphofructokinase (PFK) is a tetrameric enzyme that catalyzes a key step in glycolysis, namely the conversion of D-fructose 6-phosphate to D-fructose 1,6-bisphosphate. Separate genes encode a muscle subunit (M) and a liver subunit (L). PFK from muscle is a homotetramer of M subunits, PFK from liver is a homotetramer of L-subunits, while PFK from platelets can be composed of any tetrameric combination of M and L subunits. The protein encoded by this gene represents the L subunit. Alternate splicing results in two transcript variants, one of which is a candidate for nonsense-mediated decay (NMD).
6-phosphofructokinase, liver type
, liver-type 1-phosphofructokinase
, phosphofructo-1-kinase isozyme B
, phosphofructokinase 1
, phosphofructokinase, liver, B-type
, phosphofructokinase, liver type