Enzymes and Vitamins Overview

An oxidation reaction in organic chemistry that involves increasing the number of carbon-oxygen bonds and/or decreasing the number of carbon-hydrogen bonds.

A reduction reaction in organic chemistry that involves decreasing the number of carbon-oxygen bonds and/or increasing the number of carbon-hydrogen bonds.

An enzyme that facilitates the transfer of a functional group from one molecule to another.

A type of transferase that catalyzes the transfer of an amino group from one molecule to another.

A type of transferase that catalyzes the transfer of a phosphate group from ATP to another molecule.

The ability of an enzyme's active site to change shape slightly to better fit the substrate molecule.

The specific region on an enzyme where the substrate binds and the chemical reaction occurs.

The molecule that an enzyme acts upon.

The interactions between amino acid side chains (R groups) within an enzyme that determine its three-dimensional structure. These interactions contribute to the shape and flexibility of the active site.

The process by which an enzyme binds to its substrate, forming a temporary complex called the enzyme-substrate complex.

A dipeptide is formed when two amino acids join together by a peptide bond. This bond forms between the carboxyl group (-COOH) of one amino acid and the amino group (-NH2) of the other amino acid. A molecule of water is released during this process.

Enzymes that catalyze reactions involving the transfer of a functional group (like a phosphate group) from one molecule to another are classified as transferases.

The reaction shown involves the transfer of a phosphate group from ATP to fructose 6-phosphate, producing fructose 1,6-bisphosphate. This is a key step in glycolysis, a metabolic pathway that breaks down glucose for energy.

Phosphorylation is the process of adding a phosphate group to a molecule. This process is catalyzed by kinases, a specific type of transferase enzyme.

Kinases are a type of transferase enzyme. They play a crucial role in regulating many cellular processes by adding phosphate groups to specific molecules, often activating or deactivating them.

Increasing the concentration of the enzyme leads to a higher reaction rate, as more enzyme molecules are available to bind with substrate molecules.

Higher temperatures generally lead to faster enzyme activity, until the enzyme's optimal temperature is exceeded. Then, the enzyme's structure may be disrupted, leading to decreased activity.

Each enzyme has a specific optimal pH range where it functions best. Deviations from this optimal pH can disrupt the enzyme's structure and decrease its activity.

Increasing the substrate concentration initially boosts the reaction rate as more substrate molecules are available for the enzyme to bind with. However, the rate eventually plateaus, becoming saturated when all enzyme active sites are occupied.

The specific shape of an enzyme's active site allows it to bind to a specific substrate molecule, much like a lock and key. The enzyme then catalyzes the reaction, converting the substrate into product.

Inactive precursor of a proteolytic enzyme.

Enzyme-controlled reaction that removes part of a zymogen's structure, activating it.

Enzyme activity regulated by adding or removing a chemical group to/from the enzyme.

Adding a phosphate group to an enzyme.

Removing a phosphate group from an enzyme.

Proteolytic enzymes that digest proteins in the stomach (inactive zymogen form is pepsinogen).

The inactive precursor of pepsin, activated in the stomach by removing a peptide fragment.

A type of covalent modification where phosphate groups are added/removed from an enzyme through the formation/breaking of covalent bonds (often using ATP).

The point at which an enzyme's active sites are fully occupied by substrate molecules, leading to a maximum reaction rate.

The number of substrate molecules an enzyme converts into product per minute under ideal conditions. It measures enzyme efficiency.

The rate at which an enzyme catalyzes a reaction is directly proportional to the enzyme concentration. More enzyme means more reactions occur.

Enzymes are not consumed in the reactions they catalyze, so cells maintain a lower enzyme concentration than substrate concentration. This is efficient for the cell.

For an enzyme to function, a substrate must bind to its active site, undergo a reaction, and release the product. The cycle then repeats.

Enzymes require specific conditions (temperature, pH) to work optimally. These conditions influence their activity.

The measure of how much enzyme activity changes in response to changes in substrate concentration. It reflects the enzyme's efficiency.

Changes in temperature, pH, or other factors can affect enzyme activity by altering the shape of the enzyme and affecting its ability to bind to the substrate.