Enzymes Flashcards
Enzymes
Catalytic proteins which allow many chemical reactions within homeostasis constraints of a living system
Most are proteins except RNA
Catalyst doesn’t impact delta G, impacts free energy of activation at a moderate temperature (activation energy, Ea, energy that must be overcome for the reaction to take place)
Without enzymes, chemical traffics of various pathways of metabolism would become totally blocked
Ends often in “ase”
Are substrate specific.
Why is activation barrier essential for life
Proteins, DNA, etc are rich in free energy (G). Without Ea, everything would react (Ex ATP into ADP) fall apart
Enzyme reactions
Binds on the substrate or substrates
While they are joined, catalytic actions of the enzyme converts substrate to product
Induced fit
Substrate fitting in enzyme induces a conformation change in the enzyme
Enzyme (proteins) can move thanks to H bonds
Activation energy is lowered
Substrates are converted into products, which don’t fit so well in the enzyme and are released
Cofactors
Non protein component of enzyme, inorganic
Usually metal ions (Fe, Mg, Zn (all 2+ )
Does not bind to active site
Coenzyme
is Organic
Bind to Part of the active site
Derived from vitamins
Enzyme activity depends on
- Cofactors
- Substrate concentration
- The enzyme’s intrinsic affinity for the substrate (Km)
- Temperature
- pH
- Regulation
Concentration of enzyme and substrates
More enzymes means faster reaction
More substrate will go faster until it plateaus, enzymes are saturated
All active sites are occupied
Plateau is called v max
Km and vmax
Vmax is the plateau rate
Km is half the poteau rate
Low km has high affinity for the substrate, will often be saturate, so variation of substrate concentration will not vary a lot
And opposite, if high km, low affinity and substarte concentration will matter more
Physical conditions that influence enzyme activity
Anything that affects the bond (hydrogen, salt bridge, etc) that holds the substrate and the enzyme will affect enzyme activity
Each enzyme has optimal pH, temperature, and depends on where enzymes functions
Thermal enzymes
Responsible for distribution of colour in Siamese cats
Enzymes are only active at a certain temperature (so nose gets dark)
pH
Optimal pH
Changes enzyme activity because of denatures (low ph, carbonyl groupe gains an H, high ph, amino group lose ph
Irreversible inhibition:
Competitive inhibition that doesn’t unbind, ex penicillin
Allosteric control
molecule causes a change in enzyme shape by bonding to the enzyme at a location other than active site, activates or deactivates enzyme
Binds away from active site
Inhances or dehances, all have quaternary structure
Fixes enzyme in catalycally active or inactive position
Can be finely regulated
ex: Atp to adp is constantly changing , so ratio of atp/adp is always changing, so high adp levels causes adp to bind to enzyme which changes catalyser to activates it to produce atp, not necessary at the moment so no energy wasted
Cooperatively:
Bonding of 1 out of 4 oxygens in hemoglobin will help the binding of the second, and the third, and etc
Concentration enzyme
Regulating of enzyme activity by changing enzymes concentration or maintaining a stock of inactive enzymes and activating them when needed
Pool of enzyme that is activated when needed