Martín R, Díez V, Burgos J
Biochim Biophys Acta. 1976 Apr 8;429(2):293-300. doi: 10.1016/0005-2744(76)90277-1.
(1) The pH dependence of the kinetic parameters of the reaction catalyzed by pigeon liver diacetyl reductase (EC 1.1.1.5) was investigated in the pH range 5.1-8.6. (2) From the results obtained it is postulated that: (a), a group of pK around 7, active in the protonated form, participates in the interaction of the enzyme with NADH and NAD. (b), a second group with a pK of 8.4, active in the protonated form too, takes part in the binding of diacetyl to E-NADH. (c) A third group of pK about 4.7-5, active in the unprotonated form, is involved at least in the dissociation of the complex E-NAD and in the attachment of diacetyl to E-NADH.
(1)研究了鸽肝二乙酰还原酶(EC 1.1.1.5)催化反应的动力学参数在5.1 - 8.6 pH范围内的pH依赖性。(2)根据所得结果推测:(a),一组pK约为7的基团,以质子化形式具有活性,参与酶与NADH和NAD的相互作用。(b),第二个pK为8.4的基团,同样以质子化形式具有活性,参与二乙酰与E - NADH的结合。(c)一组pK约为4.7 - 5的基团,以未质子化形式具有活性,至少参与E - NAD复合物的解离以及二乙酰与E - NADH的结合。