Enzymes

It increases forever

It decreases to zero

It levels off as all active sites are occupied

It fluctuates up and down

pH 2

pH 8

pH 1

pH 14

Enzymes can fit any substrate if heated

One enzyme can catalyze many different types of reactions

The substrate shape is complementary to the enzyme's active site

Substrates change shape to fit into any enzyme

Pepsin

Amylase

Lipase

Trypsin

It raises the activation energy of the substrate to ensure it reacts only with the specific enzyme.

It holds the substrate in a specific orientation that strains its chemical bonds to lower the activation energy.

It provides the necessary thermal energy to the substrate to facilitate the transition state.

It causes a permanent change in the enzyme's primary structure to create the final product.

To add water to a large molecule to break it down

To remove water to join two smaller molecules together

To break the enzyme into smaller pieces

To prevent the formation of chemical bonds

To ensure enzymes are only active when needed

To prevent enzymes from turning into glucose

To make sure enzymes can only work at $100^\circ C$

To allow enzymes to be excreted as waste

$V_{max}$ is halved; $K_m$ is halved.

$V_{max}$ is halved; $K_m$ stays the same.

$V_{max}$ stays the same; $K_m$ is halved.

$V_{max}$ stays the same; $K_m$ stays the same.

Catalase increases the activation energy while $MnO_2$ lowers it.

Catalase is highly specific to $H_2O_2$, while $MnO_2$ can catalyze many different reactions.

$MnO_2$ is organic while catalase is inorganic.

Catalase is used up in the reaction but $MnO_2$ is not.

Viscosity increases the activation energy.

Viscosity slows down the diffusion of substrate and enzyme molecules, reducing collision frequency.

Viscosity changes the pH of the solution.

Viscosity causes the enzyme to unfold into its primary structure.

Substrate evaporation

Effective collisions between enzyme and substrate

Enzyme production

pH changes

Pepsin (optimum pH 2)

Trypsin (optimum pH 8)

Salivary amylase (optimum pH 7)

Lipase (optimum pH 9)

To provide energy for movement

To act as structural components of bones

To speed up metabolic reactions

To store genetic information

To make the reaction last longer

To ensure the reaction starts at the correct temperature

To prevent the substrate from dissolving

To change the pH of the solution

The enzyme will start to denature.

The reaction will slow down as the enzyme becomes too flexible.

The rate of successful collisions will increase.

The active site will become smaller.

Boiling adds too much water to the reaction.

The high temperature has permanently altered the enzyme's 3D shape.

The substrate was killed by the boiling water.

The enzyme's activation energy was removed.

The enzyme is a loose bag that can hold any substrate.

The active site slightly changes shape to fit the substrate more tightly upon binding.

The substrate changes shape to fit the enzyme's active site.

Temperature and pH dictate which substrate can enter the enzyme.

Toward a more acidic pH

Toward a more alkaline pH

It would have no effect on the optimum pH

It would make the enzyme independent of pH

It breaks all peptide bonds, releasing individual amino acids

It usually does not break the covalent peptide bonds of the primary structure

It causes the primary structure to branch into complex networks

It converts the amino acids into glucose molecules

Quaternary structure

Tertiary structure

Secondary structure

Primary structure