作者: NANCY J. GANSON , HERBERT J. FROMM
DOI: 10.1016/B978-0-12-152824-9.50026-5
关键词: Steady state (chemistry) 、 Tryptophan 、 Fructose 1,6-bisphosphatase 、 Biochemistry 、 Phosphofructokinase 、 Tetramer 、 Fructose 、 Futile cycle 、 Enzyme 、 Biology
摘要: Publisher Summary This chapter describes a study on the mechanism and regulation of bovine liver fructose-1,6-bisphosphatase (FBPase). FBPase catalyzes hydrolysis fructose 1,6-bisphosphate to form 6-phosphate (F6P) inorganic orthophosphate (Pi). Along with phosphofructokinase, enzyme plays key regulatory role in futile cycle FBP synthesis degradation. The presents studies mode at molecular level . neutral was purified shown be tetramer identical subunits native weight 140,000 ± 3000. Unlike other mammalian FBPases, seems contain least one tryptophan residue. Various kinetic constants obtained from are also compiled chapter. results reviewed show that it is possible select rapid-equilibrium random Bi-Uni as most likely possibility for reverse direction. If release products forward direction rapid equilibrium, necessary propose formation an abortive E F6P complex. However, if product instead steady state, complex need not form, but would expected inactive enzyme.