%0 Journal Article
%T Recombinant D-amino Acid Oxidase with Improved Properties<br>重组具有改良特性的D-氨基酸氧化酶
%A SV Khoronenkova
%A VITishkov
%A <br>S.V Khoronenkov
%A V.I.Tishkov
%J 生物工程学报
%D 2008
%I 
%X D-amino acid oxidase from Trigonopsis variabilis (TvDAAO) was overproduced in E. 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 ?.
%K D-amino acid oxidase
%K Trigonopsis variabilis
%K directed mutagenesis
%K X-ray structure<br>D-氨基酸氧化酶
%K 三角酵母
%K 定向诱变
%K X射线结构
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=2189139F095E203E00E54704B2D924BE&yid=67289AFF6305E306&vid=B91E8C6D6FE990DB&iid=59906B3B2830C2C5&sid=4F99DEDB606B5890&eid=6205636A05F6FF86&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=17