ENZYMES INHIBITION
Enzyme inhibitors are substance which on binding with an enzyme
decreases its catalytic activity . They may be ORGANIC or
INORGANIC in nature.
There are 3 broad categories of enzyme inhibition
1. REVERSIBLE INHIBITON
[Link] INHIBITON
3. ALLOSTERIC INHIBITON
1. REVERSIBLE INHIBITION
In this inhibition , the inhibitor is bound with the substrate with weak
non covalent bond and can be reversed if the inhibitor is removed.
It is divided into 2 types :
[Link] INHIBITION.
[Link]-COMPETITIVE INHIBITION.
A. COMPETITIVE INHIBITION
•Inhibitor closely resembles the substrate in shape. These are
known as SUBSTRATE ANALOGUE.
•Inhibitor and substrate compete for the same active site on an
enzyme.
•Inhibitor binds but does not go lysis .
•The relative concentration of the substrate and inhibitor and their
af finity to the enzyme decides the degree of inhibition. It can be
overcome if substrate concentration is high.
•Vmax Remains same but Km Decreases .
•Graph ----
Examples of competitive inhibition
1. MALONATE binding with the active site of enzyme
Succinate dehydrogenase instead of SUCCINATE .
2. METHANOL is toxic when converted to formaldehyde by
enzyme ALCHOL DEHYDROGENASE. ETHANOL can compete with
methanol for the active sites of ADH , thus can be used for
treatment of methanol poisoning.
NON-COMPETITIVE INHIBITION
• Inhibitor binds to site other than the active site .
•Inhibitor has no structural similarity with the Substrate .
• Enzymes has strong affinity for the inhibitor.
•Inhibitor don’t interfere with the enzyme – substrate binding but
don’t let
catalysis happen .
• Km value is unchanged but Vmax lowered.
EXAMPLE --- Heavy metal ions (Ag , Pb , Hg ) can non competitivly
inhibit cystilny sulfhydryl group.
[Link] INHIBITION
Inhibitor generally binds with the enzyme with covalent bond .
They are usually TOXINS .
EXAMPLE –--
•DIISOPROPYL FLOROSULPHATE is a nerve gas developed by
german in WW-II . They binds with enzyme containing serine at
their active site like serine protease , acetylcholine esterase.
•Disulfiram irreversibly inhibits Alcohol Dehydrogenase ----- makes
people sick when consumed alcohol -------- used as Treatment of
Alcoholism .
•Cynide inhibits Cytochrome oxidase and blocks ets.
•Fluoride inhibits enolase and block glycolysis.
SUICIDE INHIBITION
Speciailized form of irreversible inhibition in which the inhibitor is
converted into more potent form by the same enzyme .
The new formed inhibitor binds irreversibly with the enzyme .
EXAMPLE –
•ALLOPURINOL , is an inhibitor of xanthine oxidase , gets converted
into alloxanthine , a more effective inhibitor of the enzyme.
3. ALLOSTERIC INHIBITION
An allosteric enzyme has one catalytic site that bind to the
substrate and an allosteric site that binds to the inhibitor .
Change in the shape of the enzyme which causes change in the
shape of the active site , IF negative prevent proper binding of
substrate , thus decreasing the rate of the catalysed reaction.
