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

1. Kinetic investigations of the reaction catalysed by ATP-creatine phosphotransferase have been carried out. 2. No firm conclusions could be reached about the reaction of Mg(2+) at the nucleotide-binding site of the enzyme. The value of the kinetic constant for this reaction depends on the value used for the apparent stability constant of the metal ion-nucleotide complex and, to a smaller extent, on the method of plotting the results. 3. At higher concentrations Mg(2+) is a non-competitive inhibitor of the enzyme with respect to both MgADP(-) and phosphocreatine. 4. ADP(3-) is a competitive inhibitor of the enzyme with respect to MgADP(-) and a non-competitive inhibitor with respect to phosphocreatine. 5. The concentration of phosphocreatine has little, if any, effect on the kinetic constants for the nucleotide reactants.

biochemical journal

KINETIC STUDIES OF THE REVERSE REACTION CATALYSED BY ADENOSINE TRIPHOSPHATE-CREATINE PHOSPHOTRANSFERASE. THE INHIBITION BY MAGNESIUM IONS AND ADENOSINE DIPHOSPHATE