Cercek B, Houslay M D
Biochem J. 1982 Oct 1;207(1):123-32. doi: 10.1042/bj2070123.
There are two distinct cyclic AMP phosphodiesterases associated with the liver mitochondrion: one with the outer membrane and one with the inner membrane. No activity is associated with the lysosomal fraction. Both of the enzymes are peripheral proteins and can be released from the membranes by high-ionic-strength treatment. Treatment of intact mitochondria with trypsin and insoluble trypsin localizes these enzymes to the cytosol-facing surface of their respective membranes. The enzymes differ in regard to sedimentation coefficient, thermostability and susceptibility to inactivation by trypsin. Both enzymes degrade cyclic AMP and cyclic GMP. Whereas the outer-membrane enzyme displays Michaelis kinetics and appears to be a low-affinity enzyme, the inner-membrane enzyme displays kinetics indicative of apparent negative co-operativity.
一种与外膜相关,另一种与内膜相关。溶酶体部分没有活性。这两种酶都是外周蛋白,通过高离子强度处理可从膜上释放出来。用胰蛋白酶和不溶性胰蛋白酶处理完整的线粒体,可将这些酶定位在各自膜面向细胞质的表面。这两种酶在沉降系数、热稳定性和对胰蛋白酶失活的敏感性方面有所不同。两种酶都能降解环磷酸腺苷和环磷酸鸟苷。外膜酶表现出米氏动力学,似乎是一种低亲和力酶,而内膜酶表现出明显负协同性的动力学。