Berrocal F, Carreras J
Comp Biochem Physiol B. 1983;76(4):795-9. doi: 10.1016/0305-0491(83)90395-4.
Both treatment with diethylpyrocarbonate and photo-oxidation with rose bengal produces the loss of the three enzymatic activities of rabbit muscle phosphoglycerate mutase: phosphoglycerate mutase, glycerate-2,3-P2 synthase and glycerate-2,3-P2 phosphatase. The synthase and the phosphatase activities are less affected than the mutase activity. Glycerate-2,3-P2 and glycerate-3-P protect against diethylpyrocarbonate inactivation, but do not protect against inactivation produced by photo-oxidation. Hydroxylamine reactivates the diethylpyrocarbonate-treated enzyme. Chemical modification of phosphoglycerate mutase markedly reduces its ability to form the functionally active phosphoenzyme. These results provide evidence of the intrinsic character of the three enzymatic activities of phosphoglycerate mutase. In addition, they support the existence of two separate binding sites for monophosphoglycerates and for bisphosphoglycerates.
磷酸甘油酸变位酶、甘油酸-2,3-二磷酸合酶和甘油酸-2,3-二磷酸磷酸酶。合酶和磷酸酶活性受到的影响小于变位酶活性。甘油酸-2,3-二磷酸和甘油酸-3-磷酸可防止焦碳酸二乙酯使其失活，但不能防止光氧化导致的失活。羟胺可使经焦碳酸二乙酯处理的酶重新激活。磷酸甘油酸变位酶的化学修饰显著降低了其形成功能活性磷酸酶的能力。这些结果提供了磷酸甘油酸变位酶三种酶活性内在特性的证据。此外，它们支持存在两个分别用于单磷酸甘油酸和双磷酸甘油酸的结合位点。
