Gamblin S J, Davies G J, Grimes J M, Jackson R M, Littlechild J A, Watson H C
Department of Biochemistry, School of Medical Sciences, University of Bristol, U.K.
J Mol Biol. 1991 Jun 20;219(4):573-6. doi: 10.1016/0022-2836(91)90650-u.
The structure of the type I fructose 1,6-bisphosphate aldolase from human muscle has been extended from 3 A to 2 A resolution. The improvement in the resulting electron density map is such that the 20 or so C-terminal residues, known to be associated with activity and isozyme specificity, have been located. The side-chain of the Schiff's base-forming lysine 229 is located towards the centre of an eight-stranded beta-barrel type structure. The C-terminal "tail" extends from the rim of the beta-barrel towards lysine 229, thus forming part of the active site of the enzyme. This structural arrangement appears to explain the difference in activity and specificity of the three tissue-specific human aldolases and helps with our understanding of the type I aldolase reaction mechanism.
人肌肉中I型果糖1,6 - 二磷酸醛缩酶的结构已从3埃分辨率扩展到2埃分辨率。所得电子密度图的改善使得已知与活性和同工酶特异性相关的约20个C末端残基得以定位。形成席夫碱的赖氨酸229的侧链位于八链β桶型结构的中心。C末端“尾巴”从β桶的边缘向赖氨酸229延伸，从而形成酶活性位点的一部分。这种结构排列似乎解释了三种组织特异性人醛缩酶在活性和特异性上的差异，并有助于我们理解I型醛缩酶的反应机制。
