Unit 1 - Enzymes Flashcards
What is an enzyme
“biological catalysts” = speed up body rxn
- biological mols that catalyze or speed up rxn wout being consumed
- enzymes = proteins
- each enzyme has its own 3D shape which dictates the rxn it will catalyze.
What is an enzyme pt. 2
ends in ase
- often globular
- larger than substate
- has ACTIVE SITES
Activation Energy
in order for a rxn to proceed, particles must collide w sufficient energy. if mols collide w not enough energy, they will remain unchanged. the min amt of energy for a rxn to occur is called the AE.
Lower The Activation Energy
this means that rxn can occur at lower body temperatures if enzymes r present. this gives cells control over which rxn will occur. Not only that but since enzymes r catalysts they CAN BE REUSED.
Binding to an enzyme
- active site interacts w specific mol to catalyze specific rxn
- called a substrate
sucrose = glucose & fructose
starch = sugars
deoxynucleotide triphosphates = DNA
Models of enzymes
1) lock and key
2) induced fit model
Lock and Key model
- enzyme has an active site that is unchanging (rigid)
- substrates bind = chemical process occurs
Induced Fit Model (new)
enzyme change its shape (flexible).
IFM 1)
when a substrate enters the active site, it binds to the enzyme through many weak intermolecular bonds.
IFM 2)
the enzyme itself slightly changes shape to envelop the substrate
IFM 3)
this changes of shape can line up substrate mol and or stress chemical bonds producing the product
activation energy can be lowerd in 3 ways?
a) orientation
bring substrates in correct position
b) physical strain
make bonds weaker and easier to rearrange
c) chemical change
+ / - ions to destabilize
The catalytic cycle
since enzymes r not used up themselves in a chemical rxn they r reusable
(an enzyme binds to one or more substrate
Cofactors and Coenzymes
some enzymes need to bind to additional mols to functions
Cofactors
nonprotein inorganic substance (metal ions)
Coenzymes
nonprotein organic cofactos that r needed for some enzymes to function (shuttle btw enzymes )
ie. NAD / FAD
Apoenzyme
the enzyme without its cofactors or coenzymes
Holoenzymes
the active form bound to cofactors and coenzymes
Factor affecting enzyme activity
-concentration
-enzyme
-substrate
-temp
-ph
enzyme concentration
concentration of both the enzyme and substrate will influence the rate of a catalysis rxn.
so if there is excess substrate present then the rate of rxn is proportional to the enzyme concentration
Increasing EC
will speed up the reaction as long as there is a substrate to bind too. once all substrate is bound, the rxn will no longer speed up since there will be nothing for additionl enxymes to bind which limits the rate of rxn.
Substrate Concentration
increasin substrate concentration also increase the rate of rxn to a certain point. once all of the enzymes have bound, any substrate incease will have no effect on the rate of rxn, as the avaliable enzymes will be saturated and working at their max rate
pH and Temp
changes in pH and temp strognly affect the activity of most enxymes. enzymes usually reach max activity with a narrow range
pH
- enzymes also have optimal pH
- normal pH is 7 ; outside of this range will slow enzyme activity
-dependent on location
ie. pepsin = ph of 2
ie. trypins = ph 8 - 12
temperature
enzymes catalyzed reaction increase as temp increases
but if temp increase past a certain point, protein structure will be disrupted and enzymes will be denatured
Optimal temp
each enzyme has its own best OT.
but for most it is between 40 - 50c
humans = 37c
archaebacteria = 100c
regulation of enzyme activity
1) inhibition
2) allosterically
3) feedback inhibition
enzyme inhibitors
- lower the rate at which an enzyme catelyzes a rxn
- inhibitors r mols that bind to an enzyme and decreases its activity
competitive inhibition
- v similar in shape
- bind to the active site and physically block the correct substrate from binding
- if the concentration of inhibitor is high enough the rxn will stop
Non-Competitive inhibition
- substance that attach to a binding site on an enzyme other than active site causing a change in the enzymes shape abd loss of affinity
- may be allosteric
- inhibitor directly affects the enzyme so that it cannot carry out its function
Allosteric Regulation (2)
cells must control enzymes to coordinate cellular activities. they may accomplish this in 2 ways
1) restricting the production of a specific enzyme
2) inhibiting the action of an enzyme that had already been produced
Allosteric sites
receptor site; some distance from the active site of certain enzymes that bind substances that may inhibit or stimulate an enzymes activity.
Effector
substance that binds to the allosteric site may inhibit or stimulate and enzymes activity
Feedback inhibitor
the production of a series of enzymes catalyzed rxn acts to allosterically inhibit and enzyme that acts earlier in the series. this is an effective way to stop the synthesis of that product when aq level r produced in a cell.