The Substrate Specificity of Cyclic Imide Hydrolase Mutants / 中国生物工程杂志
China Biotechnology
; (12)2006.
Article
en Zh
| WPRIM
| ID: wpr-685487
Biblioteca responsable:
WPRO
ABSTRACT
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.
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Índice:
WPRIM
Idioma:
Zh
Revista:
China Biotechnology
Año:
2006
Tipo del documento:
Article