摘要
丙酮酸脱羧酶(pyruvate decarboxylase,PDC),EC4.1.1.1,是一种胞内酶,是焦磷酸硫胺素(thiamine pyrophosphate,ThPP)依赖性的非氧化酶,是由辅酶ThPP、Mg2+和蛋白质构成的全酶,在辅助因子焦磷酸硫胺素和Mg2+参与下作用于丙酮酸而产生乙醛和CO2。PDC是丙酮酸合成乙醇的关键酶。它广泛存在于酵母菌、霉菌、细菌和植物等多种生物体中,不同来源的丙酮酸脱羧酶的结构、相对分子质量、酶学性质等均不尽相同。该文综述了丙酮酸脱羧酶生物学性质及其应用前景。
Pyruvate decarboxylase,EC4.1.1.1,an intracellular enzyme,is a thiamine pyrophosphate-dependent non-oxidative enzyme.The holoenzyme,composed of coenzyme ThPP,Mg^2＋ and protein,catalyzes the non-oxidative decarboxylation of pyruvate to acetaldehyde using Mg^2＋ and thiamine pyrophoshate（ThPP） as cofactors.Pyruvate decarboxylase（PDC） is the key enzyme for all homo-fermentative ethanol pathways,and widely distributed among plants,yeasts,fungi,and bacteria.Pyruvate decarboxylases from different sources are not quite similar in structure,molecular weight,characterization and so on.This paper reviews the biological properties of pyruvate decarboxylase and its application.
出处
《生命科学》
CSCD
北大核心
2010年第11期1184-1191,共8页
Chinese Bulletin of Life Sciences
基金
广州市科技计划项目(10C52130100)
