NEET Botany Biology Biomolecules Enzymes MCQs

Km' = 35 μM, Vmax' = 50 μmol/min

Km' = 10 μM, Vmax' = 25 μmol/min

Km' = 25 μM, Vmax' = 50 μmol/min

Km' = 35 μM, Vmax' = 25 μmol/min

It decreases the $V_{max}$ without changing the $K_m$.

It increases the $K_m$ without changing the $V_{max}$.

It decreases both the $K_m$ and the $V_{max}$.

It increases both the $K_m$ and the $V_{max}$.

The binding of the first substrate molecule decreases the enzyme's affinity for subsequent substrate molecules.

The enzyme likely has multiple subunits.

The Hill coefficient is greater than 1.

The enzyme's activity is more sensitive to substrate concentration changes compared to enzymes with Michaelis-Menten kinetics.

$V_{max}^{app} = \frac{V_{max}}{1 + \frac{[I]}{K_i}}$

$V_{max}^{app} = V_{max}(1 + \frac{[I]}{K_i})$

$V_{max}^{app} = V_{max}$

$V_{max}^{app} = \frac{V_{max}}{K_i}$

Acting as allosteric inhibitors

Stabilizing the enzyme's structure

Participating directly in the catalytic mechanism

Facilitating substrate binding

$\frac{k_{cat}}{K_m}$

$k_{cat}$

$K_m$

$V_{max}$

The entire enzyme molecule.

The region where the substrate binds.

A non-protein component.

An inhibitor binding site.

Temperature

pH

Substrate concentration

Light intensity

Product

Substrate

Inhibitor

Cofactor

Enzyme denaturation.

The specificity of enzyme-substrate binding.

Competitive inhibition.

Allosteric regulation.