摘要
在大肠杆菌细胞中表达三角酵母D-氨基酸氧化酶,并对重组酶的性质进行了研究。制备的单一突变体与野生型酶相比,具有2.4倍的热稳定性或底物特异性变化光谱。结果显示突变的TvDAAO在氧化头孢菌素中催化效果优于野生型酶。并将一个突变的重组TvDAAO制备成结晶,并解析了2.8?分辨率下的晶体结构。
D-amino acid oxidase from Trigonopsis variabilis （TvDAAO） was overproduced in Escherichia coli cells and properties of the recombinant enzyme were studied. Single point mutants of the enzyme with 2.4-fold higher thermal stability or changed spectra of substrate specificity compared to wild-type enzyme were prepared. It was shown that mutant TvDAAO has higher catalytic efficiency in cephalosporin C oxidation in comparison with wild-type enzyme. One mutant of recombinant TvDAAO was crystallized and its structure was solved with resolution 2.8 A^°.
出处
《生物工程学报》
CAS
CSCD
北大核心
2008年第12期2125-2126,共2页
Chinese Journal of Biotechnology
关键词
D-氨基酸氧化酶
三角酵母
定向诱变
X射线结构
D-amino acid oxidase, Trigonopsis variabilis, directed mutagenesis, X-ray structure
