Cellular Energetics

Activator

Product

Substrate

Inhibitor

An increase in substrate concentration up to the point of saturation.

A substantial change in pH away from the enzyme's optimal value.

The addition of a competitive inhibitor that closely mimics the substrate.

A significant rise in temperature beyond the enzyme's optimal range.

Coenzyme deficiency.

Product accumulation.

Inhibitor concentration.

Substrate concentration.

Fermentation

Krebs cycle

Glycolysis

Photosynthesis

Crossing over during prophase I of meiosis results in recombination between homologous chromosomes.

Independent assortment during metaphase I leads each pair of homologous chromosomes separating independently.

Random fertilization creates new allele combinations when gametes unite during syngamy.

Gene duplications occurring throughout interphase produce additional copies of genes that may diverge functionally.

Inhibitors decrease the rate of reaction by preventing substrate binding or altering enzyme shape.

Inhibitors bind with substrates, decreasing their availability for reactions.

Inhibitors increase the rate of reaction by enhancing enzyme stability.

Inhibitors contribute to enzyme denaturation at high temperatures or pH levels.

Homozygous recessive for the disease allele

Homozygous dominant for the disease allele

Unable to determine without more genetic information

Heterozygous for the disease allele

Km increases while Vmax remains unchanged because more substrate concentration is required to reach half Vmax when inhibitors are present.

Neither Vmax nor Km are affected since competitive inhibitors do not alter either parameter but solely prevent substrate binding temporarily.

Vmax increases while Km remains unchanged, since competitors stimulate higher overall velocities.

Both Vmax and Km increase since competitive inhibitors permanently deactivate some amount of enzyme molecules, lowering their overall availability.

Amount of light

Temperature

Concentration of substrate

Presence of cofactors

It increases reaction rates by causing more frequent collisions between enzymes and substrates.

Temperature alters the pH level which indirectly affects enzymatic activity rather than collision frequency.

It has no effect on reaction rates as long as substrate concentration remains constant.

Temperature decreases reaction rates since enzymes become unstable at higher temperatures.