Heimer Y M, Mizrahi Y
Biochem J. 1982 Feb 1;201(2):373-6. doi: 10.1042/bj2010373.
Some characteristics of L-ornithine decarboxylase of tomato ovaries and tobacco cells are described. The enzyme has a pH optimum of 8.0. It requires pyridoxal phosphate and thiol reagent (dithiothreitol) for activity. It is specific for L-ornithine and has an apparent Km of 1.4 X 10-4 M. It has an apparent molecular weight of 107000. Putrescine inhibited the activity in vitro. Spermidine and spermine also inhibit the enzyme, but less effectively. It is concluded that the enzyme is similar to that of mammalian origin and likewise fulfils a function related to cell proliferation.
描述了番茄子房和烟草细胞中L-鸟氨酸脱羧酶的一些特性。该酶的最适pH为8.0。其活性需要磷酸吡哆醛和硫醇试剂(二硫苏糖醇)。它对L-鸟氨酸具有特异性,表观Km为1.4×10-4M。其表观分子量为107000。腐胺在体外抑制该酶的活性。亚精胺和精胺也抑制该酶,但效果较差。得出的结论是,该酶与哺乳动物来源的酶相似,同样履行与细胞增殖相关的功能。