Enzyme Catalysis Lecture Notes

A collection of vocabulary flashcards based on the lecture notes covering enzyme mechanisms, catalysis types, and related biochemical concepts.

Chemical Catalytic Mechanisms

The processes through which enzymes accelerate biochemical reactions, specifically including Acid-Base catalysis, Covalent catalysis, and Metal-ion catalysis.

Acid-Base Catalysis

A catalytic mechanism where a proton is transferred between the enzyme and the substrate.

Covalent Catalysis

A mechanism in which a covalent bond forms between the catalyst and the substrate during the transition state.

Metal-ion Catalysis

A process in which metal ions mediate oxidation-reduction reactions or enhance the reactivity of groups in the enzyme's active site.

Transition State Stabilization

The process by which enzymes lower the energy barrier of the transition state to accelerate reactions.

Induced Fit Model

The model describing how the active site of an enzyme molds itself around the substrate upon binding.

Zymogen Activation

The process where inactive precursors of enzymes are activated by cleavage, as seen in chymotrypsinogen being activated by trypsin.

Catalytic Triad

The combination of three amino acids (Aspartate, Histidine, and Serine) crucial for the catalytic activity of serine proteases like chymotrypsin.

Proximity and Orientation Effects

Effects that describe how enzymes position substrates correctly to facilitate a reaction.

Active Site

The specific region on an enzyme where substrate molecules bind and catalysis occurs.