Kallio A, McCann P P
Biochem J. 1981 Oct 15;200(1):69-75. doi: 10.1042/bj2000069.
DL-alpha-Difluoromethylornithine, an enzyme-activated irreversible inhibitor of eukaryotic ornithine decarboxylase and consequently of putrescine biosynthesis, inhibited ornithine decarboxylase in enzyme extracts from Pseudomonas aeruginosa in a time-dependent manner t1/2 1 min, and also effectively blocked the enzyme activity in situ in the cell. Difluoromethylornithine, however, had no effect on the activity of ornithine decarboxylase assayed in enzyme extracts from either Escherichia coli or Klebsiella pneumoniae. However, the presence of the inhibitor in cell cultures did partially lower ornithine decarboxylase activity intracellularly in E. coli. Any decrease in the intracellular ornithine decarboxylase activity observed in E. coli and Pseudomonas was accompanied by a concomitant increase in arginine decarboxylase activity, arguing for a co-ordinated control of putrescine biosynthesis in these cells.
DL-α-二氟甲基鸟氨酸是一种酶激活的真核鸟氨酸脱羧酶不可逆抑制剂，因此也是腐胺生物合成的抑制剂，它能以时间依赖性方式（半衰期1分钟）抑制铜绿假单胞菌酶提取物中的鸟氨酸脱羧酶，并且还能有效阻断细胞内原位的酶活性。然而，二氟甲基鸟氨酸对大肠杆菌或肺炎克雷伯菌酶提取物中检测的鸟氨酸脱羧酶活性没有影响。不过，抑制剂存在于细胞培养物中时，确实会部分降低大肠杆菌细胞内的鸟氨酸脱羧酶活性。在大肠杆菌和假单胞菌中观察到的细胞内鸟氨酸脱羧酶活性的任何降低都伴随着精氨酸脱羧酶活性的相应增加，这表明这些细胞中腐胺生物合成存在协调控制。
