%0 Journal Article
%T The substrate specificity of mutant cyclic imide hydrolases<br>突变型环酰亚胺水解酶的底物专一性
%A CHEN Yun-xia
%A NIU Li-xi
%A YUAN Jing-ming
%A SHI Ya-wei
%A <br>陈云霞
%A 钮利喜
%A 袁静明
%A 石亚伟
%J 中国生物工程杂志
%D 2007
%I 
%X The effect of C-terminal region residues on the substrate specificity of a novel cyclic imide hydrolase (CIH), a recombinant cyclic imide hydrolase (CIH293), and its mutants deleted or substituted at C-terminus (CIH291, CIH290, KK292-293EE) was reported. The substrate specificity and kinetic parameters of the mutants were analyzed by both the spectrophotometric assay and high-performance liquid chromatography. Results show that the substrate specificity of mutants was not obviously changed, but slightly low for the affinity between the substrate and enzyme, compared with the wild-type enzyme, CIH293. In conclusion, the last three residues of CIH293 play an important role for the enzyme activity.
%K Cyclic imide hydrolase Mutants Kinetic parameters Substrate specificity<br>环酰亚胺水解酶
%K 突变型酶
%K 动力学参数
%K 底物专一性
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=951380788B355DEA7D75520FA3B199C9&aid=26D1F41AF4DDA254&yid=A732AF04DDA03BB3&vid=DB817633AA4F79B9&iid=B31275AF3241DB2D&sid=D997634CFE9B6321&eid=771152D1ADC1C0EB&journal_id=1671-8135&journal_name=中国生物工程杂志&referenced_num=0&reference_num=13