溶酶体蛋白酶对肝脏醛缩酶和果糖1,6-二磷酸酶的有限水解作用：对复合物形成的影响
Limited proteolysis of liver aldolase and fructose 1,6-bisphosphatase by lysosomal proteinases: effect on complex formation.
作者信息
Pontremoli S, Melloni E, Michetti M, Salamino F, Sparatore B, Horecker B L
出版信息
Proc Natl Acad Sci U S A. 1982 Apr;79(8):2451-4. doi: 10.1073/pnas.79.8.2451.
Cathepsin M, which catalyzes inactivation of both rabbit liver fructose-1,6-bisphosphate aldolase (EC 4.1.2.13) and rabbit liver fructose 1,6-bisphosphatase (Fru-P2ase; EC 3.1.3.11), has been characterized as a peptidyl peptidase. Modification of the COOH terminus of aldolase by cathepsin M or by Fru-P2ase converting enzyme 2 abolishes its ability to bind to phosphocellulose P11 and to form the complex with Fru-P2ase. On the other hand, modification of the COOH terminus of Fru-P2ase does not affect its interaction with aldolase. This property is lost, however, when Fru-P2ase is modified in the NH2-terminal region by the converting enzyme or by subtilisin. The results suggest that interaction of aldolase and Fru-P2ase may involve the exposed COOH-terminal region of the former and an exposed proteinase-sensitive region located between residues 57 and 67 of the latter.
组织蛋白酶M可催化兔肝果糖-1,6-二磷酸醛缩酶（EC 4.1.2.13）和兔肝果糖1,6-二磷酸酶（Fru-P2ase；EC 3.1.3.11）的失活，已被鉴定为一种肽基肽酶。组织蛋白酶M或Fru-P2ase转换酶2对醛缩酶COOH末端的修饰消除了其与磷酸纤维素P11结合以及与Fru-P2ase形成复合物的能力。另一方面，Fru-P2ase的COOH末端修饰并不影响其与醛缩酶的相互作用。然而，当Fru-P2ase在NH2末端区域被转换酶或枯草杆菌蛋白酶修饰时，这种特性就会丧失。结果表明，醛缩酶和Fru-P2ase的相互作用可能涉及前者暴露的COOH末端区域和后者位于第57至67位残基之间的一个暴露的蛋白酶敏感区域。
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