Lancha A H, Recco M B, Curi R
Laboratory of Nutrition and Metabolism Applied to Motor Activity, Escola de Educação Física, Universidade de São Paulo, Brazil.
Biochem Mol Biol Int. 1994 Mar;32(3):483-9.
The mitochondrial pyruvate carboxylase catalyses the ATP-dependent carboxylation of pyruvate to oxaloacetate. Since pyruvate carboxylase generates oxaloacetate for Krebs cycle function, it is proposed that the enzyme activity may be enhanced by exercise. To investigate this proposition, pyruvate carboxylase activity was determined in the heart, soleus and gastrocnemius (white portion) muscles of sedentary and swimming-trained adult rats (1 hour per day, 5 days a week, during 5 weeks) under the following conditions: rest, one hour of exercise and exhaustion. The results show that the pyruvate carboxylase activity is increased during exercise in both the sedentary and trained groups of rats. The stimulatory mechanism is unknown but it is possibly related to the generation of pyruvate from the breakdown of glycogen and acetyl CoA during fatty acid oxidation.
线粒体丙酮酸羧化酶催化丙酮酸在ATP依赖下羧化生成草酰乙酸。由于丙酮酸羧化酶为三羧酸循环功能生成草酰乙酸,因此有人提出该酶活性可能会因运动而增强。为了研究这一观点,在以下条件下测定了久坐不动和经过游泳训练的成年大鼠(每天1小时,每周5天,共5周)的心脏、比目鱼肌和腓肠肌(白色部分)中的丙酮酸羧化酶活性:休息、运动1小时和力竭状态。结果表明,在运动期间,久坐不动组和训练组大鼠的丙酮酸羧化酶活性均有所增加。其刺激机制尚不清楚,但可能与脂肪酸氧化过程中糖原分解和乙酰辅酶A生成丙酮酸有关。