It doesn't
It doesn't
It doesn't
The rate of enzyme reaction is increased when the substrate concentration is also increased. However, when it reaches the maximum velocity of reaction, the reaction rate remains constant.
Dunno. But this is pretty cool. But if i search the question, i obvioudly don't know it, so why would i be given an optionto answer it?
In noncompetitive inhibition, the Michaelis constant (Km) remains constant because the inhibitor binds to a different site on the enzyme than the substrate, which does not affect the affinity of the enzyme for the substrate.
No, it is not true.
At equilibrium, the concentration of reactants and products remains constant, as the rates of the forward and reverse reactions are equal. The equilibrium constant (K) also remains constant at a specific temperature. The Gibbs free energy of the system is at a minimum but remains constant at equilibrium.
No, Vmax remains constant regardless of the amount of enzyme present. Vmax represents the maximum rate of reaction that can be achieved when all enzyme active sites are saturated with substrate. Once all enzyme active sites are filled, increasing the enzyme concentration further will not increase the reaction rate.
With a few exceptions, it remains relatively constant.
TRUE
The concentration of radon gas remains fairly constant because although radon decays, it is also being constantly produced from the decay of uranium and thorium in rocks and soil. This continuous production balances out the decay, leading to a relatively stable concentration of radon gas.
At a high ion concentration, the ion interfere with the bonds between the side groups of the amino acids making up the enzyme (which is a protein). This causes the enzyme to lose its shape, called denaturation. If the enzyme loses its shape, it can no longer accept and react substrate, so the rate of enzyme activity decreases.