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Enzymes
Proteins that act as catalysts to increase reaction rates without being consumed.
Active Site
A specific region in an enzyme where the substrate binds.
Transition State (TS)
The highest energy state during a reaction, where bonds are being broken and formed.
Catalysis
The process of increasing the rate of a chemical reaction by a catalyst.
Oxidoreductases
Enzymes that catalyze oxidation-reduction reactions, transferring electrons.
Transferases
Enzymes that catalyze the transfer of functional groups from one substrate to another.
Hydrolases
Enzymes that catalyze the cleavage of bonds by the addition of water.
Lyases
Enzymes that catalyze the addition or removal of groups to form double bonds.
Isomerases
Enzymes that catalyze the rearrangement of atoms within a molecule.
Ligases
Enzymes that facilitate the joining of two substrates with the use of ATP.
Acid-Base Catalysis
A catalytic mechanism where protons are transferred to stabilize transition states.
Covalent Catalysis
A catalytic mechanism involving temporary covalent bonds between the enzyme and substrate.
Metal Ion Catalysis
A form of catalysis where metal ions facilitate the reaction by stabilizing negative charges.
Enzyme Specificity
The ability of an enzyme to preferentially bind its substrate over other molecules.
Zymogens
Inactive enzyme precursors that require activation to function.
Proteolytic Activation
The process of converting inactive zymogens into active enzymes through cleavage.
Nucleophile
A chemical species that donates an electron pair to form a chemical bond.
Substrate Cleavage
The breaking of bonds in the substrate to convert it into products.
Chymotrypsin
A serine protease that cleaves peptide bonds in proteins, using a specific catalytic triad.
Peptide Bond
The covalent bond formed between amino acids in a protein.
Acyl-Enzyme Intermediate
A transient form that occurs during the enzymatic reaction where the enzyme is covalently bonded to the substrate.
Hydrophobic Pocket
A region in the enzyme that assists substrate binding through hydrophobic interactions.
Oxyanion Hole
A region in the active site of an enzyme that stabilizes the transition state by accommodating a negatively charged intermediate.