Gonzalez-Pacanowska D, García-Martinez J, García-Peregrín E
Enzyme. 1981;26(3):136-43. doi: 10.1159/000459163.
The three enzymes which catalyze mevalonic acid (MVA) phosphorylation and decarboxylation in neonatal chick brain are essentially located in the soluble fraction. The specific activity of pyrophosphomevalonate decarboxylase was the lowest of the three mevalonate-metabolizing enzymes. The rate of MVA phosphorylation and decarboxylation as a function of MVA concentration was studied. The apparent Km value of mevalonate kinase for MVA was 255 mumol/l. All three enzymes in chick brain showed a specific requirement for ATP for optimal activity. The effect of different Mg2+ concentrations was also studied. Mevalonate kinase and phosphomevalonate kinase showed maximal activity at pH 9.2 whereas pyrophosphomevalonate decarboxylase activity was highest at about pH 6.5--6.7.
在新生雏鸡脑中催化甲羟戊酸（MVA）磷酸化和脱羧反应的三种酶主要位于可溶性部分。焦磷酸甲羟戊酸脱羧酶的比活性是三种甲羟戊酸代谢酶中最低的。研究了MVA磷酸化和脱羧反应速率与MVA浓度的关系。甲羟戊酸激酶对MVA的表观Km值为255μmol/L。雏鸡脑中的这三种酶均对ATP有特异性需求以达到最佳活性。还研究了不同Mg2+浓度的影响。甲羟戊酸激酶和磷酸甲羟戊酸激酶在pH 9.2时表现出最大活性，而焦磷酸甲羟戊酸脱羧酶活性在pH约6.5 - 6.7时最高。
