作者: David N. Dietzler , Cynthia J. Lais , Mary P. Leckie
DOI: 10.1016/S0003-9861(74)80003-2
关键词: Glycogen branching enzyme 、 Biochemistry 、 Enzyme 、 Escherichia coli 、 Adenine nucleotide 、 Adenylate kinase 、 Glycogen synthase 、 In vivo 、 Biology 、 Energy charge
摘要: When exogenous nitrogen is exhausted in cultures of E. coli W4597 (K) containing excess glucose, the rate glycogen synthesis increases (3.33-fold), adenylate energy charge from 0.74 to 0.87 and FDP decreases (77%). This first observation parallel changes vivo synthesis, an increase with maintenance adenine nucleotide pool size kinase mass action ratio when growth limited. report also direct experimental evidence major elements Preiss group hypothesis concerning regulation bacterial by FDP, NADPH, PLP, primary activators ADPG pyrophosphorylase, rate-limiting enzyme this synthetic pathway. By taking into account vitro activities enzymes metabolism W4597(K) B we have concluded that decrease offset contributes increased observe, while activation NADPH improbable. Additional PLP remains a possibility discussed.