L10 Enzyme Kinetics - Allosteric Enzymes_SP25_BMM after

Initial Reaction Rate (V0)

The rate of an enzyme-catalyzed reaction measured at the start when substrate concentrations are defined.

Michaelis-Menten Enzymes

An enzyme type characterized by a hyperbolic curve relating reaction rate to substrate concentration.

Allosteric Enzymes

Enzymes that display a sigmoidal curve due to positive cooperativity, responding to substrate binding by altering their conformation.

Sigmoidal Curve

A graph shape indicating the relationship between substrate concentration and the initial reaction rate of allosteric enzymes.

Km (Michaelis constant)

The substrate concentration at which the reaction rate is half of Vmax, indicating the enzyme's affinity for the substrate.

Affinities of Enzymes

Refers to how tightly an enzyme binds to its substrate, with a lower Km value indicating higher affinity.

T-form (Tense Form)

The conformation of allosteric enzymes with a lower affinity for substrate, making them less active.

R-form (Relaxed Form)

The conformation of allosteric enzymes with a higher affinity for substrate, making them more active.

Positive Cooperativity

A phenomenon where the binding of substrate to one subunit of an allosteric enzyme increases the binding affinity of additional substrate to other subunits.

Vmax

The maximum rate of reaction achievable by an enzyme when fully saturated with substrate.

K50

A measure similar to Km, specific for allosteric enzymes, used when enzyme affinity changes along the substrate concentration curve.

Enzyme Saturation

A condition where an increase in substrate concentration does not result in an increased reaction rate, as all enzyme active sites are occupied.