Anomeric specificity of hexokinase in rat, human, and murine tumor cells.
In tumoral cells derived from the insulin-producing rat cell line RINm5F, both low- and high-Km glucose-phosphorylating enzymic activities were present. The hexokinase-like enzyme was inhibited by glucose 6-phosphate and displayed a greater affinity for but lower maximal velocity with alpha-D-glucose than beta-D-glucose. A comparable anomeric behavior of hexokinase was observed in breast cancer (MCF-7) and lymphocytic leukemia (P388) cells. Thus, the anomeric specificity of hexokinase in tumoral cells was not different from that recently characterized in normal mammalian cells.
D000818:Animals; D001943:Breast Neoplasms / Q000201:enzymology; D002460:Cell Line; D005947:Glucose / Q000378:metabolism*; D005958:Glucosephosphates / Q000494:pharmacology; D006593:Hexokinase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006801:Humans; D007328:Insulin / Q000096:biosynthesis; D007700:Kinetics; D007938:Leukemia / Q000201:enzymology; D051379:Mice; D009374:Neoplasms, Experimental / Q000378:metabolism*; D051381:Rats; D013237:Stereoisomerism; D013379:Substrate Specificity
D005958:Glucosephosphates; D007328:Insulin; D006593:Hexokinase; D005947:Glucose