Coll P M, Pérez P, Villar E, Shnyrov V L
Instituto de Microbiología Bioquímica, CSIC-Universidad de Salamanca, Spain.
Biochem Mol Biol Int. 1994 Dec;34(6):1091-8.
The application of scanning calorimetry to investigate laccase I from the lignin-degrading basidomycete PM1 (CECT 2971) showed three thermal transitions beneath the overall endotherm following the previous heating of the sample up to 60 degrees C. The thermodynamic parameters of these three transitions satisfy a model of two-state independent unfolding, supporting a three-domain organization of the enzyme. It is shown that the catalytic site of laccase I is located in the domain with the thermally-induced transition at 76 degrees C.
运用扫描量热法对木质素降解担子菌PM1(CECT 2971)中的漆酶I进行研究,结果表明,在先前将样品加热至60摄氏度后,整个吸热峰下方出现了三个热转变。这三个转变的热力学参数符合两态独立展开模型,支持该酶的三结构域组织。结果表明,漆酶I的催化位点位于76摄氏度发生热诱导转变的结构域中。