English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

Aminoacylase is inactivated by 2-ethoxy-1-(ethoxycarbonyl)-1,2-dihydroquinoline (EEDQ), a specific carboxyl reagent; inactivation is pH-dependent. The inhibition kinetics were of the first-order type. pH titration shows that half-maximal inactivation is obtained at pH 6.0 +/- 0.2, suggesting that the EEDQ reactive carboxyl group has a rather high pK value. Protection against EEDQ inactivation of the enzyme is afforded by competitive inhibitors, most effectively by tosyl-L-phenylalanine. These results suggest that a carboxyl group is located at or near the active site of the enzyme. A possible function of the carboxyl group in the catalytic process is proposed.

Inhibition of Aminoacylase from Hog Kidney by 2-Ethoxy-1-(ethoxycarbonyl)-1,2-dihydroquinoline