1887

Abstract

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.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-134-1-161
1988-01-01
2019-10-18
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-134-1-161
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error