Please wait a minute...

中国生物工程杂志

China Biotechnology
China Biotechnology  2007, Vol. 27 Issue (6): 46-50    DOI:
    
The substrate specificity of mutant cyclic imide hydrolases
Download: HTML   PDF(460KB) HTML
Export: BibTeX | EndNote (RIS)      

Abstract  

Abstract: To explore 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 mutant enzymes deleted or substituted at C-terminus (CIH291, CIH290, KK292-293EE) were prepared by gene cloning. Their substrate specificity and kinetic parameters were analyzed by both the spectrophotometric assay and high-performance liquid chromatography. Results show that the substrate specificity of mutant enzymes was not obviously changed, but slightly low for the substrate affinity, compared with the wild-type enzyme, CIH293.



Key wordscyclic imide hydrolase      mutant enzymes      substrate specificity      substrate affinity     
Received: 19 January 2007      Published: 25 June 2007
Cite this article:

. The substrate specificity of mutant cyclic imide hydrolases. China Biotechnology, 2007, 27(6): 46-50.

URL:

https://manu60.magtech.com.cn/biotech/     OR     https://manu60.magtech.com.cn/biotech/Y2007/V27/I6/46

[1] ZHU Meng-lu,WANG Xue-yu,LIU Xin,LU Fu-ping,SUN Deng-yue,QIN Hui-min. Heterologous Expression, Purification and Enzymatic Properties of a Novel Leucine 5-Hydroxylase[J]. China Biotechnology, 2019, 39(12): 24-34.
[2] Qian-qian GUO,Deng-ke GAO,Xiao-tao CHENG,Fu-ping LU,Tanokura Masaru,Hui-min QIN. Heterologous Expression, Purification and Enzymatic Characterization of Cholesterol Oxidase PsCO4[J]. China Biotechnology, 2018, 38(6): 34-42.