Enzymes
: biological catalysts (speed up reactions but are not used up in the process) made of proteins
lowers the activation energy (Ea)
Activation Energy
: the amount of energy (E) needed to start a reaction
Exergonic Reactions
: the release of E, reactants have more E than the products
Endergonic Reactions
: the storage of E, reactants have less E than the products
Enzyme Structure
are specific and only breakdown the molecule they are designed for
Lock & Key Model
: only the substrate that perfectly fits in the active site will be broken down by the enzyme
Induced Fit Model
: enzymes are slightly flexible because they are proteins and can accommodate for a
substrate that is not a perfect fit (but close)
Enzyme Inhibition
: when no substrate is present, the enzyme can be “turned off” using inhibitors
Competitive Inhibitors (Inhibitor VS Substrate)
: binds to the active site, blocking the active site from the substrate
Noncompetitive Inhibitors
: binds to the allosteric site, changing the active site’s shape so that the substrate no longer fits in it
Coenzyme
: an ion (not an enzyme) that is required to bind to an enzyme for it to function (e.g. Mg2+, Ca2+)
Factors that Affect an Enzymes Activity
Temperature
Increase
particles move faster, increasing the # of collisions between the substrate and enzyme, increasing the reaction rate
if it is too high, the enzyme will denature (because it is a protein) and stops the reaction rate
Decrease
particles move slower, decreasing the # of collisions between the substrate and enzyme, decreasing the reaction rate
pH
when outside of the enzymes optimal pH range, the enzyme denatures and stops the reaction rate
Enzyme Concentration
higher enzyme concentration will increase the reaction rate until all of the substrate is broken down
Substrate Concentration
higher substrate concentration will increase the reaction rate (because all of the substrate are grouped together) until all of the substrate is broken down
when all of the enzymes are “busy” the reaction rate will slow down