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首页> 外文期刊>Journal of Molecular Biology >FOLDING MEDIATED BY AN INTRAMOLECULAR CHAPERONE - AUTOPROCESSING PATHWAY OF THE PRECURSOR RESOLVED VIA A SUBSTRATE ASSISTED CATALYSIS MECHANISM
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FOLDING MEDIATED BY AN INTRAMOLECULAR CHAPERONE - AUTOPROCESSING PATHWAY OF THE PRECURSOR RESOLVED VIA A SUBSTRATE ASSISTED CATALYSIS MECHANISM

机译：分子内分子伴侣介导的折叠-通过基质辅助催化机制解决前体的自动加工途径。

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Subtilisin is synthesized with an N-terminal propeptide which has been demonstrated to function as an intramolecular chaperone that is only essential for the folding of the active enzyme. After folding, the propeptide is removed via an intramolecular autoprocessing mechanism. This mechanism is blocked when His64, a member of the catalytic triad is substituted with Ala. However, an additional mutation in the propeptide substituting Glu-2 with His was able to suppress the His64Ala mutation, allowing autoprocessing of the propeptide. This suppression is considered to be due to a ''substrate assisted catalysis'' mechanism and demonstrates that the cleavage to the subtilisin propeptide is an autocatalytic process. [References: 27]
机译：枯草杆菌蛋白酶与N末端前肽合成，已被证明具有分子内分子伴侣的功能，该分子伴侣仅对折叠活性酶至关重要。折叠后，通过分子内自动加工机制除去前肽。当催化三联体的一个成员His64被Ala取代时，这种机制被阻断，但是，用His取代Glu-2的前肽中的另一个突变能够抑制His64Ala突变，从而使前肽得以自体加工。这种抑制作用被认为是由于“底物辅助催化”机制所致，证明了枯草杆菌蛋白酶前肽的裂解是一种自催化过程。 [参考：27]

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