Enzyme activity: kinetics and inhibition Flashcards
Increase the rate of reaction without an enzyme
Temperature- increased number of molecules with activation energy
concentration- increase chance of molecular collisions
Enzymes
Biological catalysts that increase the rate of reaction by lowering the activation energy. Facilitate formation of transition state
Name a few important features of enzymes
Specific unchanged at reaction don't affect the reaction equilibrium increase the rate of reaction there are proteins they may require cofactors
Five features of active site
At a site is a small part of the enzyme
the active site is formed by amino acids from different parts of the primary sequence
at a site formed clefs
active site has a complimentary shape to substrate
sultry Barnes and sons by multiple weak bonds
Michaela’s menten
Rate of reaction as a functional sultry concentration
V0=Vmax x [S}
Km + [S]
Km
The substance concentration and gets half maximum velocity
Vmax
Maximum rate when all enzyme active sites are saturated with substrate
Hexokinase and glucokinase KM values
hexo found everywhere therefore has a high affinity so have a low KM. Whilst glucokinase only active when glucose level peak after feeding therefore not use all the times will have an affinity of a high KM value
Linear transformation of Michaela’s menten
Line Weaver back plot
Enzyme inhibitors
Molecules is that slow down or prevent an enzyme reaction
irreversible: bind very tightly covalent bonds
reversible: noncovalent freely dissociate
competitive- by the active site affects KM not V max
non-competitive-binds at another site on the enzyme affects Vmax but not KM
Competitive inhibition
KM increases
V Max unaffected
Non-competitive inhibitors
KM unaffected
Vmax decreases
