5.6 Enzyme Mechanisms: Chymotrypsin and Enolase

These flashcards cover key vocabulary related to enzyme mechanisms, specifically focusing on chymotrypsin and enolase, underpinning important concepts and definitions required for understanding their catalytic functions.

Chymotrypsin

A serine protease that hydrolyzes peptide bonds next to aromatic residues in dietary proteins.

Covalent Catalysis

A mechanism where an enzyme temporarily forms a covalent bond with a substrate to facilitate a reaction.

Acid-Base Catalysis

A process where proton transfer occurs to stabilize reaction intermediates and facilitate bond cleavage or formation.

Catalytic Triad

A set of three critical amino acid residues (Serine, Histidine, Aspartate) in serine proteases that enable catalytic efficiency.

Enolase

An enzyme that catalyzes the dehydration of 2-phosphoglycerate to phosphoenolpyruvate using acid-base and metal ion catalysis.

Specificity Pocket

A region in an enzyme that determines substrate specificity by providing a complementary shape and charge to the substrate.

Tetrahedral Intermediate

A transient state during enzyme-catalyzed reactions characterized by a tetrahedral geometry around a central atom.

Hydrophobic Pocket

A region in chymotrypsin's active site that preferentially binds aromatic side chains of substrates.

Nucleophilicity

The propensity of a species to donate an electron pair to an electrophile to form a chemical bond.

General Acid-Base

A catalytic mechanism where an amino acid acts as either a proton donor (acid) or acceptor (base) during a reaction.