Enzyme Kinetics and Catalysis Quiz

Enzymes facilitate biochemical reactions by reducing the energy required to initiate them.

Enzymes exhibit specificity towards particular substrates due to complementary structures and interactions.

Active sites are regions on enzymes where substrates bind and chemical reactions occur, facilitating substrate conversion.

Describes the rate of enzyme-catalyzed reactions with respect to substrate concentration.

Quantifies the efficiency of an enzyme in converting substrate to product.

Enzyme activity can be affected by various factors, but molecular weight typically does not directly influence it.

Graphical method used to analyze enzyme kinetics and determine kinetic parameters.

Enzyme inhibition involves factors that decrease enzyme activity, whereas allosteric activation increases it.

Enhances enzyme activity by promoting conformational changes or stabilizing the active form of the enzyme.

Enzyme kinetics are influenced by various factors, including temperature, pH, and substrate concentration.

Cofactors aid enzymes by facilitating chemical reactions, often by binding to the enzyme's active site.

Modulates enzyme activity by inducing conformational changes through binding at allosteric sites.

Coenzymes aid enzymes by shuttling functional groups or electrons during catalysis.

Defines the rate at which an enzyme converts substrate to product when it is fully saturated with substrate.

Regulatory enzymes control metabolic pathways by catalyzing key steps, such as hexokinase in glycolysis.

Mimic transition states of enzyme-substrate interactions, aiding in the design of inhibitors or understanding catalytic mechanisms.

Enzyme-substrate binding typically involves non-covalent interactions such as hydrogen bonds and van der Waals forces.