title: Do vanadate polyanions inhibit phosphotransferase enzymes?
abstract: Decavanadate inhibits hexokinase, adenylate kinase and phosphofructokinase; neither mono-, tri nor tetrameric vanadate anion is an inhibitor. Decavanadate inhibits phosphofructokinase obtained from bacterial and protistic sources. No form of vanadium(V) anion inhibits galacto-, glycero-, pyruvate and creatine kinase, or inorganic pyrophosphatase. Decavanadate appears to be a non-competitive inhibitor of both hexokinase substrates.
authors.forename: D W
authors.initials: DW
authors.lastname: Boyd
authors.forename: K
authors.initials: K
authors.lastname: Kustin
authors.forename: M
authors.initials: M
authors.lastname: Niwa
mesh_terms: D000818:Animals; D001412:Bacillus subtilis / Q000201:enzymology; D002175:Candida / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology; D007709:Klebsiella / Q000201:enzymology; D010770:Phosphotransferases / Q000037:antagonists & inhibitors*; D011108:Polymers / Q000494:pharmacology*; D011817:Rabbits; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012756:Sheep; D014638:Vanadates; D014639:Vanadium / Q000494:pharmacology*
chemical_list: D011108:Polymers; D014639:Vanadium; D014638:Vanadates; D010770:Phosphotransferases