most enzymes are very large molecules but only a small part of them, the ACTIVE SITE, is involved in catalysis
the active site is stereospecific
this means it binds/reacts with only 1 particular stereoisomer
the remainder of the amino acids maintain the precise shape of the enzyme and the active site
A&B are a pair of enantiomers -> non-superimposable mirror images
despite having the same shape, B doesn't fit in the stereospecific active site of the enzyme, therefore, B is not stereospecific to the active site
A fits in the stereospecific active site of the enzyme as A is stereospecific to the enzyme
the active site of an enzyme binds the substrate molecules of a biochemical reaction, and is critical to its specificity and catalytic activity
physical, e.g. temperature, or chemical, e.g. pH, factors can break the secondary and tertiary structure
if the secondary or tertiary structure of the enzyme are affected, the active site will be changed and this will affect the catalytic activity of the enzyme
enzyme inhibition
molecules that have a similar shape to the active site can compete with the reactant molecule to bond to the active site - called enzyme inhibitors
when this happens, the active site is blocked by the enzyme inhibitor and the reactant molecule cannot bond - catalysis will NOT happen at this blocked active site
the amount of inhibition depends upon the relative concentration of reactant and inhibitor
the greater the amount of inhibitor, the more active sites will be blocked
the amount of inhibitions depends on how strongly the inhibitor bonds to the active site
why use enzyme inhibition?
some antibiotics block the active site of an enzyme in bacteria which causes the cell wall to weaken and her time, the bacteria bursts
how do we develop enzyme inhibitors?
takes a lot of effort to develop a drug that fits into a stereospecific active site, often by trial and error
computers are used to model the shape of the enzyme active site and predict how well potential drugs will bind with the active site