细菌氧化还原酶烟酰型辅酶偏好性的分子机制

Molecular basis of nicotinamide coenzyme specificity of bacterial oxidoreductases

氧化还原酶因其在催化制备手性醇、羟基酸、氨基酸等方面的极大优势,在精细化工、农药、制药、食品等领域具有重要的用途。大多数氧化还原酶需要在烟酰胺类辅酶的参与下才能完成催化反应,且表现出对此类辅酶使用的偏好性。本文基于对细菌氧化还原酶和烟酰型辅酶的结构分析,总结了代表性的氧化还原酶的辅酶结合部位的结构特征以及决定辅酶偏好性的氨基酸性质,为揭示氧化还原酶对烟酰型辅酶利用偏好性的分子机制和实现辅酶偏好性改造提供依据。

Oxidoreductases can catalyze synthetic reaction ofchiral alcohols, hydroxy acid, amino acids and other aspects, and have been used extensively in producing dyes, pesticides, pharmaceuticals, food and other chemicals. Most oxidoreductases require nicotinamide coenzymes for the catalysis of reaction, and exhibit high coenzyme specificity. In this paper, the structural features of the binding site as well as the characteristics of essential amino acid residues determined the coenzyme specificity are summarized based on structure analysis of bacterial oxidoreductases and nicotinamide coenzymes, which may facilitate the understanding of molecular mechanism of cofactor preference and the structure-guided alteration of coenzyme specificity.