Hirshfield I N, Rosenfeld H J, Leifer Z, Maas W K
J Bacteriol. 1970 Mar;101(3):725-30. doi: 10.1128/jb.101.3.725-730.1970.
A mutant of Escherichia coli is described which is defective in the conversion of arginine to putrescine. The activity of the enzyme agmatine ureohydrolase is greatly reduced, whereas the activity of the other two enzymes of the pathway, the constitutive arginine decarboxylase and the inducible arginine decarboxylase, are within the normal range. The growth behavior of the mutant reflects the enzymatic block. It grows well in the absence of arginine, but only poorly in the presence of arginine. Under the former conditions, putrescine can be formed from ornithine as well as arginine, whereas under the latter conditions, because of feedback control, it can be formed only from arginine.
描述了一种大肠杆菌突变体,其在精氨酸向腐胺的转化过程中存在缺陷。胍丁胺脲水解酶的活性大幅降低,而该途径中其他两种酶,即组成型精氨酸脱羧酶和诱导型精氨酸脱羧酶的活性在正常范围内。突变体的生长行为反映了酶促阻断。它在无精氨酸的情况下生长良好,但在有精氨酸的情况下生长较差。在前一种条件下,腐胺可以由鸟氨酸以及精氨酸形成,而在后一种条件下,由于反馈控制,它只能由精氨酸形成。