Influence of the cavity structure of enzymic active sites on the selectivity for alcohol isomers from n-alkane

通过测定可溶性甲烷单加氧酶、颗粒甲烷单加氧酶、氨单加氧酶和细胞色素P450 BM-3对正构烷烃醇异构体的区域和对映电性，研究酶活性位点空腔结构对活性位点正构烷烃识别的影响。从选择性上确定了正构烷烃在酶活性位点的取向。根据所用酶的活性位点结构，我们发现正构烷烃的识别依赖于活性位点空腔的体积和组成空腔的氨基酸残基的性质。

Regio- and enantioelectivities for alcohol isomes from n-alkanes by soluble methane monooxygenase, particulate methane monooxygenase, ammonia monooxygenase, and cytochrome P450 BM-3 were measured for investigating the influence of cavity structure of enzymic active site on n-alkane recognition at the active site. From the selectivity, orientation of n-alkanes at the active site of enzymes was determined. According to the active site structure of the enzymes used here, we revealed that n-alkane recognition was dependent on the volume of active site cavity and the properties of amino acid residues composing the cavity.