Proteases and Catalysis

These flashcards cover key vocabulary regarding proteases and their mechanisms of action, including types of catalysis and specifics on various proteases.

Covalent catalysis

A catalytic strategy that involves the formation of covalent intermediates.

Acid-base catalysis

A process that uses a molecule other than water as a proton donor or acceptor.

Metal ion catalysis

A catalytic strategy where at least one-third of enzymes contain metals.

Catalysis by approximation

A strategy that involves bringing two substrates together to facilitate a reaction.

Proteases

Enzymes that cleave peptide bonds, functioning in processes such as blood coagulation and apoptosis.

Chymotrypsin

A serine protease that catalyzes the hydrolysis of peptide bonds, known for its specificity.

Cysteine proteases

Proteases that utilize a cysteine residue activated by histidine as the nucleophile.

Aspartyl proteases

Proteases that use aspartate residues to facilitate catalysis, important in regulating blood pressure.

Oxyanion hole

A region in the active site of some proteases that stabilizes the tetrahedral intermediate during catalysis.

Irreversible inhibitor

A substance that permanently disables an enzyme's activity, such as DIPF for chymotrypsin.