11-Lecture_11_3

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23 Terms

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Enzymes

Proteins that act as catalysts to increase reaction rates without being consumed.

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Active Site

A specific region in an enzyme where the substrate binds.

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Transition State (TS)

The highest energy state during a reaction, where bonds are being broken and formed.

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Catalysis

The process of increasing the rate of a chemical reaction by a catalyst.

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Oxidoreductases

Enzymes that catalyze oxidation-reduction reactions, transferring electrons.

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Transferases

Enzymes that catalyze the transfer of functional groups from one substrate to another.

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Hydrolases

Enzymes that catalyze the cleavage of bonds by the addition of water.

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Lyases

Enzymes that catalyze the addition or removal of groups to form double bonds.

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Isomerases

Enzymes that catalyze the rearrangement of atoms within a molecule.

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Ligases

Enzymes that facilitate the joining of two substrates with the use of ATP.

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Acid-Base Catalysis

A catalytic mechanism where protons are transferred to stabilize transition states.

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Covalent Catalysis

A catalytic mechanism involving temporary covalent bonds between the enzyme and substrate.

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Metal Ion Catalysis

A form of catalysis where metal ions facilitate the reaction by stabilizing negative charges.

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Enzyme Specificity

The ability of an enzyme to preferentially bind its substrate over other molecules.

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Zymogens

Inactive enzyme precursors that require activation to function.

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Proteolytic Activation

The process of converting inactive zymogens into active enzymes through cleavage.

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Nucleophile

A chemical species that donates an electron pair to form a chemical bond.

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Substrate Cleavage

The breaking of bonds in the substrate to convert it into products.

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Chymotrypsin

A serine protease that cleaves peptide bonds in proteins, using a specific catalytic triad.

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Peptide Bond

The covalent bond formed between amino acids in a protein.

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Acyl-Enzyme Intermediate

A transient form that occurs during the enzymatic reaction where the enzyme is covalently bonded to the substrate.

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Hydrophobic Pocket

A region in the enzyme that assists substrate binding through hydrophobic interactions.

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Oxyanion Hole

A region in the active site of an enzyme that stabilizes the transition state by accommodating a negatively charged intermediate.