title: Inhibition by fructose 1,6-bisphosphate of transaldolase from Escherichia coli.
abstract: The effect of fructose 1,6-bisphosphate (Fru 1,6-P2) on the regulatory enzymes of pentose phosphate pathway of Escherichia coli was examined. Fru 1,6-P2 inhibited E. coli transaldolase (EC 2.2.1.2) competitively against fructose 6-phosphate and uncompetitively against erythrose 4-phosphate, whereas Fru 1,6-P2 did not affect glucose 6-phosphate dehydrogenase (EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (EC 1.1.1.44). Kinetic results can be explained by assuming that transaldolase has two kinds of binding sites for Fru 1,6-P2: a competitive binding site for fructose 6-phosphate and a second binding site on the enzyme-erythrose 4-phosphate complex. Fru 1,6-P2 increased resulting from the stimulation of glycolysis, can inhibit transaldolase and further participates in the elevation of the concentration of ribose 5-phosphate that can be preferentially utilized for anabolic reaction in exponential phase of E. coli.
authors.affiliation: Department of Biochemistry, School of Medicine, Aichi Medical University, Yazako-Karimata 1-1, Nagakute, Aichi 480-1195, Japan.
authors.forename: Tadashi
authors.initials: T
authors.lastname: Ogawa
authors.affiliation: Department of Biochemistry, School of Medicine, Aichi Medical University, Yazako-Karimata 1-1, Nagakute, Aichi 480-1195, Japan.
authors.forename: Keiko
authors.initials: K
authors.lastname: Murakami
authors.affiliation: Department of Biochemistry, School of Medicine, Aichi Medical University, Yazako-Karimata 1-1, Nagakute, Aichi 480-1195, Japan yoshino@aichi-med-u.ac.jp.
authors.forename: Masataka
authors.initials: M
authors.lastname: Yoshino
mesh_terms: D001665:Binding Sites; D001667:Binding, Competitive; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism*; D005635:Fructosediphosphates / Q000378:metabolism* / Q000494:pharmacology; D005636:Fructosephosphates / Q000494:pharmacology; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism; D006019:Glycolysis / Q000187:drug effects; D007700:Kinetics; D010427:Pentose Phosphate Pathway / Q000187:drug effects*; D010734:Phosphogluconate Dehydrogenase / Q000378:metabolism; D012267:Ribosemonophosphates / Q000378:metabolism; D013403:Sugar Phosphates / Q000494:pharmacology; D014153:Transaldolase / Q000037:antagonists & inhibitors* / Q000378:metabolism
chemical_list: D005635:Fructosediphosphates; D005636:Fructosephosphates; D012267:Ribosemonophosphates; D013403:Sugar Phosphates; C031626:ribose-5-phosphate; C026959:erythrose 4-phosphate; C027618:fructose-6-phosphate; D010734:Phosphogluconate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase; D014153:Transaldolase; C029063:fructose-1,6-diphosphate
keywords: E. coli; Fru 1,6-P2; fructose 1,6-bisphosphate; inhibition; pentose phosphate pathway; transaldolase