Newaz S S, Hersh L B
J Bacteriol. 1975 Nov;124(2):825-33. doi: 10.1128/jb.124.2.825-833.1975.
Comparison of enzyme activities in crude extracts of methylamine-grown Pseudomonas MA (ATCC 23319) to those in succinate-grown cells indicates the involvement of an acetyl coenzyme A-independent phosphoenolpyruvate carboxylase in one-carbon metabolism. The purified phosphoenolpyruvate carboxylase is activated specifically by reduced nicotinamide adenine dinucleotide (KA = 0.2 mM). The regulatory properties of this enzyme suggests that phosphoenolpyruvate serves as a focal point for both carbon assimilation and energy metabolism.
将甲胺培养的甲基营养型假单胞菌MA（ATCC 23319）粗提取物中的酶活性与琥珀酸培养细胞中的酶活性进行比较，结果表明，一种不依赖乙酰辅酶A的磷酸烯醇式丙酮酸羧化酶参与了一碳代谢。纯化后的磷酸烯醇式丙酮酸羧化酶被还原型烟酰胺腺嘌呤二核苷酸特异性激活（KA = 0.2 mM）。该酶的调控特性表明，磷酸烯醇式丙酮酸是碳同化和能量代谢的焦点。
