lecture 5 - enzymes

what is the purpose of an enzyme

they enable our metabolic processes to occur at useful times by speeding up reactions

what is specificity

enzymes can only bind to their specific substrate using specificity residues within the active site

what is geometric complementarity

the substrate physically fits in the active site

what is electronic complementarity

charges, partial charges, H-bonding, N.P groups that are within the enzyme to go with the substrate

what are the two ways an enzyme can speed up a reaction

they make molecules more reactive by adding acid or base or they can out opposite charges or partial charges next to the unstable charges.

what are catalytic residues

they enable the reaction by placing groups in places to stabilize unstable transition states

what are cofactors/coenzymes

they help enable necessary enzymatic reactions

what are enzyme kinetics

in an enzyme kinetic we measure the activity of the enzyme under different conditions

what is initial velocity conditions

measuring enzymatic reaction rates early before there is very much product present so that no product can be converted into substrate

what is Vmax

the maximum velocity is the top speed at which product can be made in an enzymatic reaction when substrate concentration is starting.

what is KM

this is also known as Michaelis constant and it is the substrate concentration needed for the enzyme to operate at 50% of Vmax. It tells us how well the enzyme binds to the substrate

what are Lineweaver-Burk Plots

its a double reciprocal plot

what are competitive enzymes

the inhibitor binds in the active site and blocks the substrate from binding. If the inhibitor unbinds the substrate can bind.

what is a non-competative

the inhibitor binds somewhere else on the enzyme and causes the enzyme to stop working