Thimann Laboratories, University of California, Santa Cruz, California 95064.
Plant Physiol. 1979 Apr;63(4):687-91. doi: 10.1104/pp.63.4.687.
ATP citrate lyase (EC 4.1.3.8) has been found in crude extracts from endosperm tissue of germinating castor bean and shows its maximum activity in 4- to 5-day-old seedlings. A strict requirement for coenzyme A and adenosine 5'-triphosphate was demonstrated. The pH optimum for the reaction is around 7.5. The unstable enzyme can be stabilized by freezing and addition of citrate and glycerol. (-)-Hydroxycitrate is a potent inhibitor. The molecular weight is about 400,000. The adenosine 5'-triphosphate citrate lyase is localized in the plastids, where it possibly plays a role in providing acetyl coenzyme A for lipid biosynthesis.
三磷酸柠檬酸裂合酶(EC 4.1.3.8)在发芽蓖麻胚乳组织的粗提物中被发现,并在 4 至 5 日龄的幼苗中表现出最大活性。证明该酶对辅酶 A 和腺苷 5'-三磷酸有严格的要求。反应的最适 pH 值约为 7.5。不稳定的酶可以通过冷冻和添加柠檬酸和甘油来稳定。(-)-羟基柠檬酸是一种有效的抑制剂。分子量约为 400,000。三磷酸柠檬酸裂合酶定位于质体中,可能在为脂质生物合成提供乙酰辅酶 A 方面发挥作用。