Motoki K, Kitajima Y, Hori K
Department of Biochemistry, Saga Medical School, Japan.
J Biol Chem. 1993 Jan 25;268(3):1677-83.
Vertebrate aldolase molecules bear at least four stretches of isozyme group-specific sequences (referred to as IGS). The IGSs of the type A isozyme are known to endow the aldolase molecules with some characteristics typical of A. In order to locate the type A regions, 4 chimeric enzymes were constructed between human aldolases A and B and 5 mutant enzymes with single or double mutations in the IGS-1 region. Among engineered proteins, the chimeric enzymes bearing the type A IGS-1 to -4 (BABA34-108:306-363) and the IGS-1 and -4 (BABA34-55:306-363) exhibited similarities to isozyme A in many respects. On the other hand, neither chimeric enzyme bearing the type A IGS-1 to -3 (BAB34-108) nor that bearing the IGS-1 alone (BAB34-55) exhibited properties as isozyme A. Four mutant aldolases A (carrying single mutation in the IGS-1 region) maintained the original activity as A. Similarly, the BA306 chimera with the type B-->A substitution at positions 41 and 45 (BA306 N41K:R45S) failed to exhibit the A-like properties although the activities toward Fru-1,6-P2 and Fru-1-P significantly increased. Conclusively, the type A IGS-1, together with the IGS-4, act as indispensable modules in determining the characteristic properties of human aldolase A.
脊椎动物醛缩酶分子至少有四段同工酶组特异性序列(称为IGS)。已知A型同工酶的IGS赋予醛缩酶分子一些典型的A特性。为了定位A型区域,构建了4种人醛缩酶A和B之间的嵌合酶以及5种在IGS-1区域有单突变或双突变的突变酶。在工程蛋白中,带有A型IGS-1至-4(BABA34-108:306-363)和IGS-1及-4(BABA34-55:306-363)的嵌合酶在许多方面表现出与同工酶A相似。另一方面,带有A型IGS-1至-3(BAB34-108)的嵌合酶和仅带有IGS-1(BAB34-55)的嵌合酶均未表现出同工酶A的特性。四种突变醛缩酶A(在IGS-1区域有单突变)保持了A的原始活性。同样,在第41和45位具有B型到A型取代的BA306嵌合体(BA306 N41K:R45S)尽管对Fru-1,6-P2和Fru-1-P的活性显著增加,但仍未表现出A样特性。总之,A型IGS-1与IGS-4一起,在决定人醛缩酶A的特性方面起着不可或缺的作用。