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

Dedicated to Prof. H. Zahn on the Ocassion of His 65th Birthday Zn+2/Co+2 Exchange, Microbial Acylamino Acid Amido Hydrolase, Aspergillus oryzae, Kinetic Properties The inactivation of the Zn+2 metallo enzyme acylamino acid amido hydrolase from Aspergillus oryzae by ethylendiamine-tetraacetate (EDTA) and nitrilotriacetate (NTA) and the effects of Phe and His on this process were studied. Reactivation of the enzyme by Zn+2-or Co+2-NTA buffer revealed a dissociation constant for the Zn+2-enzyme of 10~10 M and for the Co+2-enzyme of 10-7-5 m. The kinetic properties of the Zn+2 and Co+2 enzyme were compared for a series of substrates. Substitution of Co+2 for Zn+2 reduces substrate specificity of the enzyme.

Co +2 -Substituted Acylamino Acid Amido Hydrolase from Aspergillus oryzae