The substrate specificity of mutant cyclic imide hydrolases
突变型环酰亚胺水解酶的底物专一性

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.