Chymotrypsin Overview

Flashcards covering key terms and concepts related to chymotrypsin and its role as a protease.

Chymotrypsin

A serine protease enzyme that hydrolyzes peptide bonds in proteins.

Protease

An enzyme that cleaves peptide bonds in proteins.

Chymotrypsinogen

The inactive precursor of chymotrypsin produced in the pancreas.

Active Site

The region of an enzyme where substrate molecules bind and undergo a chemical reaction.

Covalent Intermediate

A transient species resulting from a covalent bond formed during chemical reactions, particularly in enzyme catalysis.

Nucleophilic Substitution

A type of chemical reaction in which a nucleophile forms a bond with a carbon atom, replacing another atom or group.

Catalytic Triad

A set of three amino acids (usually Ser, His, and Asp) in the active site of serine proteases that work together to enhance reaction efficiency.

Oxyanion Hole

A region within the active site of some enzymes that stabilizes a tetrahedral intermediate, containing a negatively charged oxygen atom.

Peptide Bond

The chemical bond formed between amino acids in proteins.

Turnover Number (kcat)

The number of substrate molecules converted to product by an enzyme in a given time when the enzyme is fully saturated.