Department of Biology, Rensselaer Polytechnic Institute, Troy, New York 12181.
Plant Physiol. 1975 Jun;55(6):975-7. doi: 10.1104/pp.55.6.975.
An enzyme was extensively purified from jack bean leaves (Canavalia ensiformis L.) which produced o-ureidohomoserine from l-canaline and carbamyl phosphate. The most highly purified preparations catalyzed both this reaction and citrulline synthesis from ornithine and carbamyl phosphate, and the ratio of the two activities remained nearly constant during purification. When hydrated jack bean seeds were the enzyme source, ornithine carbamyltransferase (EC 2.1.3.3) activity was high but synthesis of ureidohomoserine was barely detectable. Both ornithine carbamyltransferase and the ureidohomoserine synthesizing enzyme had similar Km values for carbamyl phosphate. The purification data suggest that one enzyme may catalyze both reactions in jack bean leaves.
从刀豆(Canavalia ensiformis L.)叶片中大量纯化出一种酶,该酶能将 l-瓜氨酸和氨甲酰磷酸转化为 o-脲基高丝氨酸。最高度纯化的制剂能催化这两种反应,以及从鸟氨酸和氨甲酰磷酸合成瓜氨酸,并且在纯化过程中,这两种活性的比例几乎保持不变。当水合的刀豆种子是酶的来源时,鸟氨酸氨甲酰转移酶(EC 2.1.3.3)活性很高,但几乎检测不到脲基高丝氨酸的合成。鸟氨酸氨甲酰转移酶和合成脲基高丝氨酸的酶对氨甲酰磷酸具有相似的 Km 值。纯化数据表明,一种酶可能在刀豆叶片中催化这两种反应。