3.1.4.2 Many proteins are enzymes Flashcards
Enzymes as a catalyst
- enzymes decrease activation energy (minimum energy to start the reaction)
- to increase the rate of reaction
Specificity of proteins (enzymes/antibodies)
- tertiary structure of the
- active site/ variable region is
- complimentary to the shape of the substrate and forms an
- enzyme-substrate complex/ antibody-antigen complex
Non-functional proteins
e.g. mutation changes 1ᵒ structure
e.g. denaturation changes ionic bonds
-→changes 3ᵒ structure
-changes shape of active site
-substrate not complimentary
=no e-s complex
Induced fit model of enzyme action
-enzyme and substrate are not exactly complimentary
-so enzyme changes shape slightly so substrates fit
-substrate changes shape slightly
└=bonds break more easily
└=lower activation energy
Lock and key model of enzyme action
-enzyme and substrate are exactly complimentary
=enzyme substrate complex →enzyme product complex
Factors effecting enzyme activity
pH
-pH is altered =denature enzyme =change in 3D/ 3ᵒ structure └due change in charge distribution / hydrogen and ionic bonds affected -changes specific shape of active site =substrate not complimentary to enzyme =substrate cannot fit and bind to the active site =e-s complexes not formed -this decreases enzyme activity =decrease rate of reaction
Factors effecting enzyme activity
Temperature
Optimum temperature -increase kinetic energy =increase frequency and energy of collisions =increase E-S complexes =max rate of reaction achieved
Higher than optimum temperature -increase kinetic energy =increase frequency and energy of collisions =enzyme vibrates too much =breaks hydrogen binds =change in 3D/ 3ᵒ structure =substrate not complimentary to enzyme =substrate cannot fit and bind to the active site =e-s complexes not formed -this decreases enzyme activity =decrease rate of reaction
Factors effecting enzyme activity
Enzyme concentration
-increase enzyme concentration
-increase number of active sites available
└as long as there are enough substrates to fill them
-this increases enzyme activity / e-s complexes
=increase rate of reaction
└until substrate is used up (becomes a limiting factor)
Factors effecting enzyme activity
Substrate concentration
-increase substrate concentration
-increase number of substrates available to fill active sites
└as long as there are enough active sites for them to fill
-this increases enzyme activity/ e-s complexes
=increase rate of reaction
└until there are no more active sites available (becomes a limiting factor)
Factors effecting enzyme activity
Competitive inhibitor
-inhibitor has a similar shape to the substrate
└= complimentary/ can fit in active site for a short time
=prevents the substrate from entering the active site.
-less effect if more substrate is added
Factors effecting enzyme activity
Non-competitive inhibitor
-inhibitor fits into a site other than the active sit (allosteric site) =alters shape/charge of active site =change in 3D/ 3ᵒ structure =substrate not complimentary to enzyme =substrate cannot fit and bind to the active site =e-s complexes not formed -this decreases enzyme activity =decrease rate of reaction -reaction won’t reach maximum
-increasing substrate concentration has no effect