Kinetic properties of CqJHE for ρ-nitrophenyl acetate, α-naphthyl acetate, and JH IIIa.

aThe enzyme was purified by ion exchange chromatography as described in the text. The values given assume that the purity of the enzyme preparation (i.e., the 150 mM NaCl fraction after ion exchange) was 48%, and were corrected for background hydrolysis. The results shown are the mean ± standard deviation of at least three separate experiments.bThe assays were performed in 50 mM sodium phosphate buffer, pH 7.4, at 30°C.cThe assays were performed in glycine-sodium hydroxide buffer, pH 9.0, at 30°C.