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 Plus annual

Presents the access of premium content as premium feature

Premium Content

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 annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The activity of an enzyme involved in decyanation of cyanocobalamin was found in the cell homogenate of Euglena gracilis. The enzyme essentially required FAD or FMN, and NADPH as cofactors. The apparent Km for cyanocobalamin and NADPH were 7.1 microM and 0.2 mM, respectively. The enzyme reaction obeyed allosteric kinetics towards FAD ([FAD]0.5 = 30 microM, n = 2.7; as calculated by the Hill plots). The Euglena enzyme was located in the mitochondria.

Occurrence and characterization of cyanocobalamin reductase (NADPH; CN-eliminating) involved in decyanation of cyanocobalamin in Euglena gracilis.