SUMMARY: The -caprolactone hydrolases (EC 3.1.1-) induced by growth of NCIB 9871 and CL1 with cyclohexanol were purified to homogeneity. Both enzymes constituted approximately 1% of the soluble protein of the bacteria. Each was formed from two electrophoretically indistinguishable subunits and each had a closely similar value (⋍60000). Both enzymes had high turnover numbers typical of carboxyesterases, broad pH-activity spectra and very restricted substrate specificities. In contrast to other bacterial lactone hydrolases they catalysed irreversible lactone hydrolysis and were not inhibited by thiol-reactive compounds. Their sensitivity to Paraoxon (diethyl -nitrophenylphosphate) suggested that they, in common with mammalian acetylcholinesterase and carboxyesterases, have a functional catalytic centre serine.


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