Studies on the structure and function of enzymes related to C-S bond formation and cleavage of useful naturally-occuring cyclic compounds having sulfur

首次研究了与天然重要环状化合物的C-S键形成和裂解有关的嗜热酶的结构和功能。目标酶是参与生物素(维生素H)合成途径第一步的KAPA合成酶(BioF)，作为与C-S成键途径相关的模型酶；以及参与石油中的空气污染物二苯并噻吩单氧酶(DBT)，作为与C-S键断裂途径相关的模型酶。对于前者，其温度特性和底物专一性明显优于已知的中温微生物。对于后一种酶，从应用的角度来看，发现了一个有用的新反应。

The structure and function of thermophilic enzymes related to C-S bond formation and cleavage of naturally occuring important cyclic compounds were studied for the first time. Targeted enzymes are KAPA synthase(BioF), which is involved in the first step of biotin(vitamin H) synthetic pathway, as the model enzyme related to C-S bond formation pathway, and dibenzothiophene(DBT) monooxigenase(BdsC), which is involoved in the first and second steps of DBT, an air pollutant contained in petroleum, as the model enzyme related to C-S bond cleavage pathway. As for the former enzyme, the temperature properties and substrate specificities were significantly superior to those of known mesophilic organisms. As for the latter enzyme, a useful new reaction was found in terms of application.