At what substrate concentration would this enzymatic reaction be operating at only 20 percent of its maximum rate?

One of the hallmarks of competitive inhibition is that there is constant competition betweenthe substrate and the inhibitor for binding to the enzyme active site.a) If [inhibitor] >> [substrate], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?b) If [substrate] >> [inhibitor], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?

In the pathway for degradation of BCAAs, which reaction takes place prior to the action of the BCKDC and what is the essential coenzyme for the reaction?

Describe the rate of enzyme-catalyzed reaction with increasing  substrate concentration at constant enzyme concentration. In what ways does hydrogen ion concentration affect enzyme activity?

The enzymatic activity of an enzyme with Kg = 2 mM that converts substrate S into product P is measured at an initial substrate concentration S, of 10 µM. After 5 min, the substrate concentration is halved. What is the rate constant k, the maximal velocity vmax and the concentration of product after 12 min?

a) Based on the data shown in the image, what are the Km and Vmax for the enzyme with L-DOPA and D-DOPA? Show any relevant analyses or calculatins you did to determine these values. ( HINT a graph might be helpful here! )  b) Based on your answer to part a, briefly describe how the kinetics of the enzyme differs for the two substrates. Which Substrate has better binding affinity to the enzyme