Enzymes Flashcards
1.7, 1.8, 1.9
enzymes are……
- biological catalysts
- They are substrate specific (complementary)
enzymes are effective in….
tiny amounts
enzymes are______ proteins at the _______ structure
globular, tertiary
catalyses reactions both ___________ (in cell) and __________ (outside cell) which determines structure/function
intracellular, extracellular
enzymes are catabolic what does that mean?
active site effects bonds in substrate, substrate breaks (hydrolysis)
what does anabolic mean?
bring substrate molecules together (building, condensation)
How should a typical reaction should occur:
- ______ collide with enzyme with sufficient ______ energy.
- alters arrangement of _____
- energy of ______ must be lower than energy of _______
substrate, kinetic
atoms
products, substrate
how do enzymes speed up chem reactions?
lower activation energy (reactions can occur at lower temps)
what is the area the substrate fits into on a protein called?
the 3D active site
what is the name given when a substrate interacts with an enzyme?
enzyme-substrate complex
Describe the induced fit model
- enzyme is flexible + alters shape in presence of substrate (due to change of environment)
- enzyme puts strain on substrate
- causes distortion in substrate bond(s) = lowers activation energy
Describe the outdated lock + key model
the shape of the substrate exactly fits into the active site
name the 5 factors that affect enzyme action
pH, temp, substrate conc., enzyme conc., conc. of competitive and non-competitive inhibitors
how is the rate of an enzyme controlled reaction measured?
- rate of formation of products
- rate of disappearance of substrate
Describe an enzyme reaction in 6 steps
- at first easy for substrate to come into contact with enzyme (lots of empty sites)
- substrate rapidly broken down = increase in product
- less and less substrate = harder to come into contact with enzyme
- takes longer for substrate to be broken down = rate of formation + disappearance decreases
- reaction slows
- graph flattens = all substrate used up
how to measure rate of change? (graph)
measuring gradient at certain point (may need a tangent)
How does a rise in temp affect enzyme activity?
increases kinetic energy, more collisions = more enzyme-substrate complexes
what happens when you exceed optimum temp/pH of the enzyme?
denaturation of 3D active site = no enzyme-substrate complexes = decrease in rate
how does pH affect how an enzyme works?
- can change amino acids making up active site
- can cause breakage of bonds in enzyme tertiary structure (changes active site)
what aids in determining the active site?
the ionic bonding between NH2 (amine) and COOH (carboxyl)
enzymes work well at low conc. because…
are not used up in a reaction
what happens when enzyme conc. is low?
- excess substrate molecules
- not enough active sites
- rate only half of max for no. of substrate
what happens when there’s intermediate enzyme conc.?
- all substrate molecules occupy active sites
- rate at max. as all sites filled
what happens when there’s high enzyme conc.?
- already enough enzymes to accommodate substrate
- no increase in rate of reaction