Determine the value of the turnover number of the enzyme carbonic anhydrase, given that Ras for carbonic anhydrase equals 249 µmol L and [E], 2.38 nmol L, Carbonic anhydrase has a single active site.
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.
K 4
![The turnover number is defined as the maximum number of substrate molecules that can be converted into product molecules
per unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily equal to the concentration of
enzyme molecules, because some enzyme molecules have more than one active site. If the enzyme molecule has one active site.
the turnover number is given by
turnover number
Rmax
[E]
=k₂ (Rmax is often written as Vmax)
If the enzyme molecule has more than one active site, then [E], is multiplied by the number of active sites to determine its
effective concentration.
turnover number=
Determine the value of the turnover number of the enzyme carbonic anhydrase, given that Rmax for carbonic anhydrase equals
249 µmol-Land [E], 2.38 nmol L Carbonic anhydrase has a single active site.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fa73ae55a-26b6-4048-8111-ba5b495985cc%2F4ff938b4-fa24-4187-9501-eaab5046bdbc%2Fq52gabx_processed.jpeg&w=3840&q=75)
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