Michaelis constant K_m is equal to: | vedclass

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Question

(B) In the Michaelis-Menten enzyme kinetics model,the reaction is represented as $E+S \underset{K_2}{\stackrel{K_1}{\rightleftharpoons}} E S \xrightar

Vedclass · Accepted Answer

$\frac{K_2 + K_3}{K_1}$

Vedclass · Answer

(B) In the Michaelis-Menten enzyme kinetics model,the reaction is represented as $E+S \underset{K_2}{\stackrel{K_1}{\rightleftharpoons}} E S \xrightarrow{K_3} E+P$
Here,$K_1$ is the rate constant for the formation of the enzyme-substrate complex,$K_2$ is the rate constant for the dissociation of the complex back into enzyme and substrate,and $K_3$ (often denoted as $k_{cat}$) is the rate constant for the formation of the product.
The Michaelis constant $K_m$ is defined as the substrate concentration at which the reaction rate is half of the maximum velocity $(V_{max})$.
Mathematically,it is expressed as $K_m = \frac{K_2 + K_3}{K_1}$.

Column-$I$	Column-$II$
$a$. Transferase	$i$. Aldolase
$b$. Hydrolase	$ii$. Alcohol dehydrogenase
$c$. Lyase	$iii$. Sucrase
$d$. Oxidoreductase	$iv$. Glucokinase

Michaelis constant $K_m$ is equal to:

Similar Questions

Lactic dehydrogenase $(LDH)$,which catalyzes the conversion of pyruvate to lactate,is an example of:

Select the correct option for the processes given below.

What binds to the active site of an enzyme?

$A$: Life is not possible without proteins.
$R$: All enzymes are made of proteins.

Match Column-$I$ and Column-$II$ with reference to enzymes and select the correct option.
Column-$I$ Column-$II$
$a$. Transferase $i$. Aldolase
$b$. Hydrolase $ii$. Alcohol dehydrogenase
$c$. Lyase $iii$. Sucrase
$d$. Oxidoreductase $iv$. Glucokinase

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