Ovchinnikova M V, Mikhailova A G, Karlinsky D M, Gorlenko V A, Rumsh L D
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str. 16/10, Moscow, 117997, Russia.
Moscow State Pedagogical University, M. Pirogovskaya Str. 1, bldg. 1, Moscow, 119991, Russia.
Acta Naturae. 2018 Apr-Jun;10(2):65-70.
A unique property was found for oligopeptidase B from (PSP) as well as its mutants: they can undergo reversible thermal inactivation at 37°C, with activity being restored or even increased with respect to the initial one upon subsequent cooling. The process can be repeated several times, with the same results achieved (up to 5 cycles). This effect can be explained by a shift in the equilibrium between the inactive open form of the enzyme and the active closed one upon variation of the incubation temperature.
发现来自（PSP）的寡肽酶B及其突变体具有一种独特的特性：它们在37°C时可发生可逆的热失活，随后冷却时活性相对于初始活性得以恢复甚至增加。该过程可重复多次，每次都能得到相同的结果（最多5个循环）。这种效应可以通过孵育温度变化时酶的无活性开放形式和活性封闭形式之间的平衡发生转变来解释。
