酵素之分子辨識及受質特異性

The Molecular Recognition and the Substrate Specificity of Enzyme

鄭建業(Chean-Yeh Cheng)

《化學》 51卷3期 (1993/09) Pp. 320-323

https://doi.org/10.6623/chem.1993034

摘要

酵素為生物性催化劑與非生物性催化劑之不同處即在於酵素具有分子辨識能力形成受質特異性。酵素對分子之辨識乃基於酵素－受質複合體中結合點的多寡。古典理論要求至少三點之結合才能達到辨識的功能，但根據許多例證顯示大分子受質需要以多點（超過三點）和酵素結合才可達到受質特異性。而對稱性小分子則可利用二點以下之結合達成分子辨識之目的。非對稱性小分子如能藉輔因子之存在或酵素－受質複合體之結構穩定度亦能以二點以下之結合而有分子辨識能力形成受質特異性。

並列摘要

Enzyme is a biocatalyst and is different from the non-biocatalyst in possessing molecular recognition to form substrate specificity. The molecular recognition of enzyme is based on the number of point attachments in the enzyme-substrate complex. Classically, at least three-point attachment is needed to fulfill the molecular recognition. However, there are many evidences to clue that macromolecules need multi-point attachment (more than three-point attachment) with enzyme to obtain substrate specificity, small symmetry molecules may use two-point attachment or even one-point attachment to get molecular recognition, and small asymmetry molecules together with the cofactor or the stability of enzyme-substrate complex can also use two-point attachment or one-point attachment to have molecular recognition.