Pepsin is an enzyme in the stomach that digests proteins. Because it is active in the stomach, which is highly acidic, pepsin best functions at a low pH between 2 and 2.5.

Pepsinogen is secreted by chief cells and converted into active pepsin after catalyzation by hydrochloric acid. The acid is secreted by parietal cells in response to gastrin secretion by G cells. After the stomach contents enter the duodenum of the small intestine, the acid is neutralized by bicarbonate secretions from the pancreas. This prevents the acid from damaging the walls of the small intestine.

Inhibitors are able to prevent maximum enzymatic rates in a variety of ways. Some inhibitors, like noncompetive inhibitors, are able to attach at a point on the enzyme and alter its conformation. Competitive inhibitors, however, bind directly at the active site, which prevents substrate from entering the enzyme.

Competitive inhibitors are the only inhibitor type to bind directly to the enzyme actve site.

Proteins have the most diverse functions in biological systems. Their remarkable diversity in function is due to their diversity in structure. Structural proteins, such as tubulin and collagen, have a fibrous structure that aids their function. Enzymes have active sites that allow them to bind specific molecules (substrates) and enact a conformational change to facilitate chemical reactions. Signaling proteins include several types of hormones, known as peptide hormones. Protein receptors are commonly found embedded in the cell membrane and contain active sites to bind substrates, hydrophilic regions to interact with the cell environment and extracellular space, and hydrophobic regions to interact within the lipid bilayer.

Inhibitors are able to prevent maximum enzymatic rates in a variety of ways. Some inhibitors, like noncompetive inhibitors, are able to attach at a point on the enzyme and alter its conformation. Competitive inhibitors, however, bind directly at the active site, which prevents substrate from entering the enzyme.

Competitive inhibitors are the only inhibitor type to bind directly to the enzyme actve site.

Pepsin is an enzyme in the stomach that digests proteins. Because it is active in the stomach, which is highly acidic, pepsin best functions at a low pH between 2 and 2.5.

Pepsinogen is secreted by chief cells and converted into active pepsin after catalyzation by hydrochloric acid. The acid is secreted by parietal cells in response to gastrin secretion by G cells. After the stomach contents enter the duodenum of the small intestine, the acid is neutralized by bicarbonate secretions from the pancreas. This prevents the acid from damaging the walls of the small intestine.

Proteins have the most diverse functions in biological systems. Their remarkable diversity in function is due to their diversity in structure. Structural proteins, such as tubulin and collagen, have a fibrous structure that aids their function. Enzymes have active sites that allow them to bind specific molecules (substrates) and enact a conformational change to facilitate chemical reactions. Signaling proteins include several types of hormones, known as peptide hormones. Protein receptors are commonly found embedded in the cell membrane and contain active sites to bind substrates, hydrophilic regions to interact with the cell environment and extracellular space, and hydrophobic regions to interact within the lipid bilayer.

Keratin is a fibrous protein found in hair, nails, and the epidermis of skin. Myosin is one of the major proteins of muscle. Trypsin is an enzyme in the small intestine that helps digest proteins. Collagen is a fibrous protein found in connective tissue, such as bone and cartilage. Fibrin is a clotting protein found in the blood in response to injury.

Keratin is a fibrous protein found in hair, nails, and the epidermis of skin. Myosin is one of the major proteins of muscle. Trypsin is an enzyme in the small intestine that helps digest proteins. Collagen is a fibrous protein found in connective tissue, such as bone and cartilage. Fibrin is a clotting protein found in the blood in response to injury.

A competitive inhibitor will temporarily bind to the active site on an enzyme. This forbids substrates from entering the enzyme's active site and stops the enzyme from catalyzing the reaction.

In contrast, non-competitive inhibitors will bind to other regions of the enzyme, outside of the active site, and cause the active site to change shape. This change then prevents substrates from binding.

A noncompetitive inhibitor does not directly compete with the substrate binding to the substrate-binding site of an enzyme. The inhibitor instead binds to another site on the enzyme, which alters the enzyme's affinity for its substrate; therefore, adding more substrate would not cause a change in enzymatic activity.