UDP-glucose pyrophosphorylase 2 (UGP2)

UDP-glucose pyrophosphorylase 2 (UGP2) catalyzes the conversion of glucose-1-phosphate and UTP to UDP-glucose, a crucial intermediate in glycogen biosynthesis and protein N-glycosylation[1][2][3]. UGP2 is the sole enzyme for this reaction in mammals, directly affecting energy metabolism and cellular signaling. UGP2 is regulated by pathways including YAP–TEAD and is implicated in cancer cell survival, growth, and metastasis, mainly in pancreatic ductal adenocarcinoma, where high UGP2 expression correlates with poor prognosis[1]. Loss or inhibition of UGP2 impairs glycogen synthesis and protein glycosylation, especially for receptors such as EGFR essential for cancer proliferation[1]. Therapeutic targeting poses risks due to the enzyme’s universal metabolic importance; careful modulation rather than complete inhibition may be necessary for clinical viability[1][2].

Other names

UTP--glucose-1-phosphate uridylyltransferaseUGP2UGP1UDPGPUGPaseUGPP1SVUGP2UDP-glucose pyrophosphorylaseDEE83EIEE83UDPGUDPGP2UGPP2pHC379UDP-glucose diphosphorylaseUDP-glucose pyrophosphorylase 1UGPase 2UTP--glucose-1-phosphate uridylyltransferase 2Uridyl diphosphate glucose pyrophosphorylase-1testis tissue sperm-binding protein Li 58puridyl diphosphate glucose pyrophosphorylase 2

Drugs targeting UGP2 would likely inhibit UDP-glucose synthesis, affecting glycogen synthesis and glycosylation pathways; inhibition can decrease cell survival and proliferation, especially in cancer cells dependent on UGP2-mediated metabolism