Characterization of intracellular esterase A from Bacillus subtilis.
Esterase A (EC 3.1.1.1) obtained by sonic disruption of Bacillus subtilis SR22 (spoA12, trpC2) was purified approximately 400-fold by differential chemical and heating precipitation, DEAE-cellulose chromatography, and Bio-Rad P-150 gel filtration chromatography, with an overall yield of 59%. The purified enzyme hydrolyzed both aliphatic and aromatic acetate esters at substrate concentrations of 0.25 M but did not hydrolyze amino acid esters. Aliphatic alcohols did not inhibit the hydrolysis of p-nitrophenyl acetate; the most potent inhibitors of esterase activity were mercuric chloride, diisopropylfluorophosphate, eserine, and sodium fluoride.
D001412:Bacillus subtilis / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D004237:Diuron / Q000494:pharmacology; D004355:Drug Stability; D005459:Fluorides / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008628:Mercury / Q000494:pharmacology; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D010830:Physostigmine / Q000494:pharmacology; D013329:Structure-Activity Relationship
D010664:Phenylmethylsulfonyl Fluoride; D004237:Diuron; D010830:Physostigmine; D002265:Carboxylic Ester Hydrolases; D008628:Mercury; D005459:Fluorides