Proteins (enzymes) Flashcards
how are enzymes biological catalysts (3 marks)
- lower activation energy
- by providing alternate route
-speed up reaction
draw graph for w/ catalyst vs w/o (1 marks)
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describe induced fit model on enzyme action (4 marks)
- substrate binds to active site
-causing active site to change shape so its complementary to substrate - so enzyme-substrate complex forms
-causing bonds in substrate to bend, lowering activation energy
induced fit vs lock and key (2 marks)
-lock and key says active site ids fixed shape lock and substrate is key fits easily
-induced fit, active site changes shape to be complementary to substrate
what determines the function/ activity of a enzyme (2 marks)
- primary structure (sequence of amino acids) determines function
-tertiary structure determines shape of active site
explain specificity of enzymes (3 marks)
-tertiary structure determines shape of active shape
-active shape is complementary to substrate
-only this substrate can bind to active fit, induced fit and form E-S complex
explain how enzyme concentration affects the rate of reaction (6 marks)
talk about conc, limiting factor, collisions
-Increasing enzyme conc. → rate of reaction increases.
-Enzyme conc. = limiting factor (substrate in excess).
-More enzymes → more available active sites.
-More successful E-S collisions and E-S complexes.
-At a certain point, rate of reaction plateaus.
-Substrate conc. = limiting factor (all substrates in use).
explain how substrate concentration affects the rate of an enzyme-catalysed reaction (5 marks)
talk about limiting factor, collsiions, plateaus
-Increasing substrate conc. → rate of reaction increases.
-Substrate concentration = limiting factor (too few enzyme molecules to occupy all active sites).
-More successful E-S collisions and E-S complexes.
-At a certain point, rate of reaction plateaus.
-Enzyme conc. = limiting factor (all active sites saturated; excess substrate).
explain how temperature affects the rate of an enzyme-catalysed reaction (6 marks)
talk about optimum temp, collsisions, bonds
-Increasing temp. up to optimum → rate of reaction increases.
-Increase in kinetic energy.
-More successful E-S collisions and E-S complexes.
-Increasing temp. above optimum → rate of reaction falls.
-Enzymes denature; tertiary structure and active site change shape (hydrogen and ionic bonds break).
-Fewer E-S collisions and E-S complexes (substrate no longer binds to active site).
-Rate of reaction 0 when all enzymes denatured.
explain how pH affects the rate of an enzyme-catalysed reaction (5 marks)
talk about optimum ph, bonds, collisions
-pH above/below optimum pH → rate of reaction decreases.
-Enzymes denature; tertiary structure and active site change shape
-hydrogen and ionic bonds break
-Complementary substrate no longer binds/fits to active site.
-Fewer E-S collisions and E-S complexes.
explain how concentration of competitive inhibitors affects the rate of an enzyme-catalysed reaction (5 marks)
talk about induced fit,e-s complex, effect of increasing sub conc of inhibitor
- decrease rate of reaction
-Similar shape to substrate.
-Competes for / binds to / blocks active site so substrates can’t bind.
-Fewer E-S complexes.
-Increasing substrate conc. reduces effect of inhibitor (level of inhibition dependent on relative concs. of substrate and inhibitor).
explain how concentration of non-competitive inhibitors affects the rate of an enzyme-catalysed reaction. (6 marks)
talk about active site, e-s complex, effect of increasing sub conc on rate of reaction
-decrease rate of reaction.
-Binds to site other than the active site (allosteric site).
- changes Enzyme tertiary structure
-so substrate can’t bind to active site.
-Fewer E-S complexes.
-Increasing substrate concentration has no effect on rate of reaction as causes permanent change to active site.
draw graph for effect of enzyme conc on rate of enzyme controlled reaction
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draw graph for effect of substrate conc on rate of enzyme controlled reaction
check google
draw graph for effect of temperature on rate of enzyme controlled reaction
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draw graph for effect of pH on rate of enzyme controlled reaction
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draw graph for effect of competitive and non-competitive inhibitors on rate of enzyme controlled reaction
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