Michaelis-Menten analysis of enzyme kinetics has some limitations about the conditions under which it can be applied. These include all of the following except one-choose the one that is not true. O The kinetics must be analyzed in the early part of the time course (i.e. measuring the initial velocity), before product has accumulated to a significant level. O The concentration of the enzyme-substrate complex is constant. O The concentration of the enzyme-substrate complex (ES) is greater than 50% of total enzyme. The turnover number (kcat) for an enzyme is O the number of times it can catalyze a reaction before it dies. O the maximum number of substrate molecules that the enzyme can bind at one time. O the maximum rate at which the enzyme's active site can catalyze the reaction. O the number of times the enzyme can roll over and play dead before you have to give it a treat.
Catalysis and Enzymatic Reactions
Catalysis is the kind of chemical reaction in which the rate (speed) of a reaction is enhanced by the catalyst which is not consumed during the process of reaction and afterward it is removed when the catalyst is not used to make up the impurity in the product. The enzymatic reaction is the reaction that is catalyzed via enzymes.
Lock And Key Model
The lock-and-key model is used to describe the catalytic enzyme activity, based on the interaction between enzyme and substrate. This model considers the lock as an enzyme and the key as a substrate to explain this model. The concept of how a unique distinct key only can have the access to open a particular lock resembles how the specific substrate can only fit into the particular active site of the enzyme. This is significant in understanding the intermolecular interaction between proteins and plays a vital role in drug interaction.
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