The specific pocket on an enzyme where the substrate binds and the reaction takes place.
The active site is a cleft lined with specific amino acids that bind the substrate through weak interactions and catalyse the reaction using catalytic residues. Only a small part of the enzyme forms the site; the rest maintains its shape.
Specificity arises from the complementary shape, charge and hydrophobicity.
The specific pocket on an enzyme where the substrate binds and the reaction takes place.
Active Site is one of the 51 topics in Biomolecules & Biochemistry. It is rated Intermediate, so it suits learners who already know the core vocabulary. Related topics in this area include Induced Fit Model, Noncompetitive Inhibition, Tertiary Structure.
The serine protease active site uses a catalytic triad of serine, histidine and aspartate.
Work through the Beginner topics in Biomolecules & Biochemistry first, such as Water Properties, Carbon Chemistry, Carbohydrates, then return to Active Site. Intermediate topics assume the Beginner vocabulary.
The closest topics to Active Site are Induced Fit Model, Noncompetitive Inhibition, Tertiary Structure, Michaelis-Menten Kinetics. Comparing them side by side is a good way to see how the ideas connect.
Read the summary and the in-depth section, then use the quick check on the interactive lesson for Active Site. To practise the whole of Biomolecules & Biochemistry, use the Biomolecules & Biochemistry quiz.
Active Site: The specific pocket on an enzyme where the substrate binds and the reaction takes place. Induced Fit Model: Suggests the enzyme's active site changes shape slightly as the substrate binds, improving the fit. Read both side by side and note what each one explains.
First, read the summary and write the definition in your own words. Second, read the in-depth section and note any example. Third, compare it with Induced Fit Model and explain the difference aloud. Finally, take the Biomolecules & Biochemistry quiz and come back to this page for any question you miss.
Suggests the enzyme's active site changes shape slightly as the substrate binds, improving the fit.
⚗️ Biomolecules & BiochemistryAn inhibitor binds elsewhere on the enzyme, lowering Vmax without changing Km.
⚗️ Biomolecules & BiochemistryThe overall three-dimensional shape of one polypeptide, held by side-chain interactions and disulfide bridges.
⚗️ Biomolecules & BiochemistryModels reaction velocity as Vmax times substrate over Km plus substrate, describing enzyme saturation.
⚗️ Biomolecules & Biochemistry