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What is Vmax
Vmax is the maximum rate of an enzymatic reaction when the enzyme is saturated with substrate. It represents the point at which adding more substrate will not increase the reaction rate.
What is Km
Km is the substrate concentration at which the reaction rate is half of Vmax. It reflects the affinity of the enzyme for its substrate.
What is the relationship between Km and enzyme-substrate affinity
Inversely related, as Km increases, enzyme-substrate affinity decreases
How are line-weaver burke plots read?
y-intercept is the inverse of Vmax, x-intercept is the negative inverse of Km. For both axes, closer to 0 is higher Vmax and Km
what is competitive enzyme inhibition
the inhibitor competes for the active site, can be overcome by increasing substrate concentration. This results in a higher Km (lower E-S affinity) without affecting Vmax.
what is non-competitive inhibition
inhibitor binds to allosteric site to change enzyme shape. Has equal affinity for enzyme and enzyme-substrate complex. Results in decreased Vmax and equal Km
what is uncompetitive inhibition
inhibitor only binds to the enzyme-substrate complex, preventing conversion to product. This decreases both Vmax and Km, produces a line-weaver burke plot with parallel lines
what is mixed inhibition
inhibitor binds to the allosteric site but either prefers the enzyme or the ES complex. Both lower Vmax. If preference for enzyme, Km increases, if preference for ES complex, Km decreases
what is an apoenzyme
an enzyme that does not have the cofactor it needs to work
what is a holoenzyme
an ezyme with the cofactor it requires to be active.
what is the difference between a cofactor and a coenzyme
a coenzyme is an organic molecule that helps the enzyme carry out its function, a cofactor is an inorganic molecule or ion that helps an enzyme carry out its function