Enzyme Kinetics

Questions and Answers

To act as biological structures for cellular processes

To catalyze chemical reactions and transform substrates (correct)

To serve as inhibitors of substrate reactions

To act as the main energy source in cells

It measures the energy released during enzymatic reactions

It assesses the efficiency of enzyme catalysis over time (correct)

It identifies the genetic makeup of enzymes

It determines the structural attributes of proteins

pH levels

Temperature

Substrate concentration

The enzyme's genetic sequence (correct)

Glycolytic enzymes Signup and view all the answers

It decreases the amount of substrate converted to product Signup and view all the answers

Glyceraldehyde-3-phosphate Signup and view all the answers

By serving as allosteric regulators Signup and view all the answers

The 3-D structure and active sites Signup and view all the answers

Different enzymes that catalyze the same reaction Signup and view all the answers

The rate at which they saturate with substrates Signup and view all the answers

Study Notes

Enzymes are proteins with unique structures that are folded to create 3-D active/catalytic sites, enabling specific recognition of substrates that they transform.
Enzymes are biological catalysts that increase the rate or velocity of chemical reactions without being changed in the overall process.
Enzymes lower the activation energy, allowing chemical reactions to proceed faster.

Lysozyme is an example of Transition State Theory.
The Induced Fit Model proposes that substrate binding distorts the substrate into a conformation close to the transition state.
In the Induced Fit Model, substrate binding can also induce conformation changes to the enzyme.
Hexokinase is an example of the Induced Fit Model, where the binding of glucose causes two protein domains to close together, closing the binding cleft.

Enzyme kinetics is the study of the rates of enzyme-catalyzed reactions.
The rate of the reaction is affected by temperature, pH, and substrate concentration.
The rate of the reaction is reflected by the slope of the curve, while the enzyme capacity is reflected by the height of the curve.
Saturation of the enzyme with substrate is reached at Vmax, where the enzyme converts substrates into products at its maximal rate.
Km is the substrate concentration at which the enzyme converts substrates into products at half its maximal rate, reflecting the affinity of the substrate for the enzyme.

Oxidoreductases (Class I) catalyze oxidation-reduction reactions.
Transferases (Class II) catalyze the transfer of groups between molecules.
Hydrolases (Class III) catalyze the cleavage of bonds coupled with inserting water.
Lyases (Class IV) catalyze the cleavage of carbon-carbon, carbon-sulphur, and carbon-nitrogen bonds.
Isomerases (Class V) catalyze the rearrangement of bonds.
Ligases (Class VI) catalyze the formation of bonds between carbon and oxygen, sulfur, or nitrogen.