Glycosylation (“gly-KAH-sih-LAY-shun”) of this enzyme’s serine-529 attenuates its activity, conferring a growth advantage to tumor cells with higher glycosylation rates. AKT (“act”) stabilizes tetramers of overrepresented “platelet” subunits of this enzyme in tumors that upregulate its activity to adapt to hypoxia (“hy-POX-ee-uh”). In normal tissues, this enzyme contains varying numbers of platelet, muscle, and liver subunits. (-5[1])Insulin-activated protein phosphatase (“FOSS-fuh-tace”) activates the second isoform of this enzyme to create an allosteric activator of this enzyme’s first isoform. The reaction catalyzed by this enzyme is reversed by FBPase (-5[1])(“F-B-P-ace”). This enzyme’s main (10[1])isoform is allosterically (10[1])activated by AMP (10[1])and (-5[1])phosphate or (10[2])inhibited by citrate (10[1]-5[1])and ATP to prevent a futile cycle with gluconeogenesis (“GLOO-koh-NEE-oh-jen-eh-sis”). For 10 points, name this enzyme that catalyzes the (-5[1])first (10[1]-5[2])[emphasize] committed (10[1]-5[1])step (-5[2])of glycolysis (-5[1])by phosphorylating (-5[1])fructose-6-phosphate. (0[1]) (10[5]0[4]) ■END■