Paper Report for: Kim_2004_J.Mol.Catal.B.Enzym_27_237
Reference
Title: Occurrence of ofloxacin ester-hydrolyzing esterase from Bacillus niacini EM001. Kim HK, Na HS, Park MS, Oh TK, Lee TS Ref: J Mol Catal B Enzym, 27:237, 2004 : PubMed
A Bacillus niacini strain (EM001) producing an ofloxacin ester-enantioselective esterase was isolated from the soil samples collected near Taejon, Korea. The cloned gene showed that the esterase EM001 composed of 495 amino acids corresponding to a relative molecular weight (Mr) of 54,098 kDa. Based on the Mr and the protein sequence, the esterase EM001 was similar to p-nitrobenzyl esterase from Bacillus subtilis with an identity of 41.8%. The optimum temperature and pH of the purified His-tagged enzyme were 45 degC and 9.0, respectively. The purified esterase EM001 hydrolyzed preferably (R)-ofloxacin propyl ester than (S)-form ester at the initial reaction phase with an eeP of 67% until the conversion rate become up to 35%.
Kim HK, Na HS, Park MS, Oh TK, Lee TS (2004) Occurrence of ofloxacin ester-hydrolyzing esterase from Bacillus niacini EM001. J Mol Catal B Enzym27: 237-241
Kim HK, Na HS, Park MS, Oh TK, Lee TS (2004) J Mol Catal B Enzym27: 237-241