Tucker G A, Dawson A P
Biochem J. 1979 Jun 1;179(3):579-81. doi: 10.1042/bj1790579.
The kinetic mechanisms of the beta-hydroxybutyrate dehydrogenase from rat heart and liver mitochondria were investigated. Both enzymes, show an Ordered Bi Bi mechanism and there are no major differences in the kinetic constants. In both cases, the solubilized enzyme, re-activated with phosphatidylcholine, shows kinetic properties very similar to those of the enzyme bound to the mitochondrial membrane.
对大鼠心脏和肝脏线粒体中β-羟基丁酸脱氢酶的动力学机制进行了研究。这两种酶均表现出有序的双底物双产物机制,动力学常数没有显著差异。在这两种情况下,用磷脂酰胆碱重新激活的可溶性酶表现出与结合在线粒体膜上的酶非常相似的动力学性质。