309288
Descrição
Mapa Mental por kathrynmoar, atualizado more than 1 year ago
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Criado por kathrynmoar
mais de 10 anos atrás
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Enzyme Kinetics
- when an enzyme is incubated with substrates the reaction rate decreases
over time either because of substrate depletion or product inhibition
- initial rate = Vo
- if the initial rate is measured the reaction velocity is
linearly related to the amount of enzyme
- Michaelis-Menton
- proposes = rate of reaction is determined by the rate of
formation of enzyme-substrate complex at low substrate
concentrations but eventually something other than the ES
complex becomes limiting
- constant Km = concentration of substrate at which the rate is half maximal
- 1/V against 1/S gives a straight line from which
Km can be determined as can Vmax.
- provided that the dissociation rate of the enzyme-substrate
complex is much greater than the rate of formation of products
Km represents the dissociation constant.
- most enzymes in the cell operate at substrate conc below Km
- typical values = 10 to the minus 4 and 10 to the minus 6 M
- typical values = 10 to the minus 4 and 10 to the minus 6 M
- 1/V against 1/S gives a straight line from which
Km can be determined as can Vmax.
- constant Km = concentration of substrate at which the rate is half maximal
- high substrate conc. = all enzyme is present as ES and
enzyme is saturated with substrate. Rate of reaction = Vmax.
- an enzyme following this with velocity against
substrate plotted will have a hyperbolic shape
- an enzyme following this with velocity against
substrate plotted will have a hyperbolic shape
- proposes = rate of reaction is determined by the rate of
formation of enzyme-substrate complex at low substrate
concentrations but eventually something other than the ES
complex becomes limiting
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