Cronan J E
J Bacteriol. 1980 Mar;141(3):1291-7. doi: 10.1128/jb.141.3.1291-1297.1980.
The enzyme, aspartate 1-decarboxylase (L-aspartate 1-carboxy-lyase; EC 4.1.1.15), that catalyzes the reaction aspartate leads to beta-alanine + CO2 was found in extracts of Escherichia coli. panD mutants of E. coli are defective in beta-alanine biosynthesis and lack aspartate 1-decarboxylase. Therefore, the enzyme functions in the biosynthesis of the beta-alanine moiety of pantothenate. The genetic lesion in these mutants is closely linked to the other pantothenate (pan) loci of E. coli K-12.
在大肠杆菌提取物中发现了一种酶,即天冬氨酸1-脱羧酶(L-天冬氨酸1-羧基裂解酶;EC 4.1.1.15),它催化天冬氨酸生成β-丙氨酸 + CO₂ 的反应。大肠杆菌的panD突变体在β-丙氨酸生物合成方面存在缺陷,并且缺乏天冬氨酸1-脱羧酶。因此,该酶在泛酸的β-丙氨酸部分的生物合成中发挥作用。这些突变体中的基因损伤与大肠杆菌K-12的其他泛酸(pan)基因座紧密连锁。