大肠杆菌K-12鸟氨酸脱羧酶、精氨酸脱羧酶和胍丁胺脲水解酶缺失突变体中多胺的生物合成
Biosynthesis of polyamines in ornithine decarboxylase, arginine decarboxylase, and agmatine ureohydrolase deletion mutants of Escherichia coli strain K-12.
作者信息
Panagiotidis C A, Blackburn S, Low K B, Canellakis E S
出版信息
Proc Natl Acad Sci U S A. 1987 Jul;84(13):4423-7. doi: 10.1073/pnas.84.13.4423.
Abstract
Escherichia coli K-12 mutants that carry deletions in their genes for ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) (speC), arginine decarboxylase (L-arginine carboxy-lyase, EC 4.1.1.19) (speA), and agmatine ureohydrolase (agmatinase or agmatine amidinohydrolase, EC 3.5.3.11) (speB) can still synthesize very small amounts of putrescine and spermidine. The putrescine concentration in these mutants was found to be 1/2500th that in spe+ cells. The pathway of putrescine synthesis appears to be through the biodegradative arginine decarboxylase, which converts arginine to agmatine, in combination with a low agmatine ureohydrolase activity--1/2000th that in spe+ strains. These results suggest that even such low levels of polyamines permit a low level of protein synthesis. Evidence is presented that the polyamine requirement for the growth of the polyamine-dependent speAB, speC deletion mutants, which are also streptomycin resistant, is not due to a decreased ability to synthesize polyamines.
摘要
携带鸟氨酸脱羧酶（L-鸟氨酸羧基裂解酶，EC 4.1.1.17）（speC）、精氨酸脱羧酶（L-精氨酸羧基裂解酶，EC 4.1.1.19）（speA）和胍丁胺脲水解酶（胍丁胺酶或胍丁胺脒水解酶，EC 3.5.3.11）（speB）基因缺失的大肠杆菌K-12突变体仍能合成极少量的腐胺和亚精胺。这些突变体中的腐胺浓度被发现仅为spe+细胞中的1/2500。腐胺的合成途径似乎是通过生物降解性精氨酸脱羧酶将精氨酸转化为胍丁胺，并结合低水平的胍丁胺脲水解酶活性——仅为spe+菌株中的1/2000。这些结果表明，即使是如此低水平的多胺也能支持低水平的蛋白质合成。有证据表明，对多胺依赖性speAB、speC缺失突变体（它们也对链霉素耐药）生长所需的多胺，并非由于合成多胺的能力下降。
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