Carbonic Anhydrase(CA)

Presented by,
Riniya Najeeb
CARBONIC ANHYDRASE

• Carbonic Anhydrase is a enzyme which

accelerates the conversion of carbon
dioxide into carbonates
• Carbonic Anhydrase is capable of turning
carbon dioxide molecules into carbonates
at a rate of one million molecules per
second
0VERVIEW
 Enzymes are biological catalysts that accelerates
chemical reactions
 Such as the conversion of gaseous carbon dioxide
into carbonates
 Carbonic Anhydrase is a type of enzyme that
rapidly catalyses the conversion of carbon dioxide
into a proton and the bicarbonate ion(HCO3-)
 The reaction is rather slow in the absence of
Anhydrase catalyst, as the reaction with the
enzyme takes place typically 10^4-10^6 times per
second
In humans this reaction mechanism is vital in
maintaining pH balance and in transporting
co2 out of the tissues and into the lungs

Effect of pH on carbonic anhydrase activity

STRUCTURE
 In CA, as well as all biological systems,
the zinc atom is in the +2 state
 The zinc is bound to four ligands,three of
its coordination sites are occupied by the
imidazole ring of three hisitidine residues
and a forth is occupied by a water
molecule.
 The active site is located in a cleft near
the center of the enzyme
 FUNCTION

Mechanism of carbon dioxide converted to carbonic acid

CA is a catalytic enzyme specific to

accelerating the formation of carboic acid
from carbon dioxide and water
 It is important that the CA does not shift the
equilibrium of the reaction but rather helps the
equilibrium be reached much quicker, allowing for its
high velocity yield of product.
 H2CO3 dissociate in blood, which gives this
equilibrium

 CA has been known to catalyze one million reactions

per sec
 Also CA readily dissociates into H++ and
bicarbonates since it is a more stable compound
MECHANISM
 pH affects carbonic anhydrase in a sigmoidal
fashion
 Higher the pH, the more active the enzyme
is(since it is in the optimal condition for
deprotonation)
1. The binding of zinc lowers the pKa of water,
generating OH- ions to attack carbon dioxide.
Zinc release a proton from a water molecule to
generate this hydroxide ion. pH decreases as a
result from the decrease in pKa. According to
Le chatelier’s principle, this drives the reaction
towards deprotonation.
2. The CO2 substrate binds to the enzyme active
site and is positioned for optimal interaction
3. The OH- ion attacks the carbonyl of carbon
dioxide, converting it to bicarbonate ion. Oxygen
on the carbon dioxide molecule forms an
intermediate bond with the Zn metal during the
conversion process
4. The enzyme is regenerated and the bicarbonate
ion is released. The enzyme is ready for another
reaction to occur.
SPECIFIC CASES OF CARBONIC ANHYDRASE
 CA can be used when carbon dioxide in the tissue
diffuses into human RBC. The CO2 react with
water to form carbonic acid. Typically this
reaction is catalyzed by CA

CO2---enter red blood cellCO2+H2O---

catalyzed by carbonic anhydraseH2CO3
 A case of reducing the activity of CA is found in a
class of drugs used to treat glaucoma,
neurological disorders, and ulcers.
 REFERENCE

1. BERG,JEREMY M (2007),BIOCHEMISTRY,6TH
Ed., Sara Tenney
2. Campbell, Neil A ,BIOLOGY.7TH Ed. San
francisco,2005