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中文摘要：
利用同源模建和分子动力学模拟方法，模建了大肠杆菌中高丝氨酸琥珀酰基转移酶的三维结构，分析了活性位点的组成，从结构上佐证了Cys142而不是Lys47为亲核进攻的残基，并通过与其天然底物琥珀酰-辅酶A的对接研究，从理论上确认了对复合物形成起到重要作用的氨基酸残基。
英文摘要：
The three dimensional structure of homoserine transsuccinylase from Escherichia coli （EcHTS） was modeled by using homology and molecular dynamics methods. On the basis of the modeling, the components of active site in EcHTS were analyzed. The structure analysis shows that Cys142 but not Lys47 is the main residue for the nucleophile during the catalytic reaction. The docking of succinyl-CoA with EcHTS has also been performed, and the important residues for binding were identified.
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