CHAPTER 1

BIO150
 CONTENTS:
N ZY
Factors Effecting Enzyme
05 Activity

06 Cofactor
 COFACTOR
Some enzymes require non protein components for their efficient activity.

The protein component referred as apoenzymes and the non protein

component is known as cofactors.
Shape up either the enzyme or the substrate into a shape that causes ESC to
be produced.
Probability of a reaction occur will increase and the rate of reaction will also
increase.

3 types cofactor:
Coenzyme; Prosthetic group; Metal ions
 Coenzyme
 Small, non protein organic cofactor.
Coenzyme

 Binds loosely and temporarily to the active

site of the enzyme.

 They are readily detach and can be

classified as transfer agents where they Your Picture Here
transfer chemical group, atoms, or
electron from one enzyme to another.

 Example: NAD (nicotinamide adenine

dinucleotide)
 FUNCTION OF
activity
COENZYMES
• A coenzyme prepares the active site for catalytic
 Prosthetic Group

Organic cofactor.

Binds tightly and permanently to the enzyme.

FAD : Flavin adenine dinucleotide.

Enzyme –protein portion (apoenzyme)
haloenzyme
+
Nonprotein component (cofactors)
 Metal Ions
Inorganic cofactor.

E.g. K+, Zn2+, Mg2+, Co2+,

Fe2+,Mn2+

It alters the shape of enzyme.

They attach to the enzyme temporarily

 Enzyme Components
A holoenzyme is the enzyme that has the cofactor.
A apoenzyme is the enzyme without cofactor.
 COFACTOR
Non-protein components that bound tightly or loosely
Required by certain enzyme for their efficient activity

Coenzyme Prosthetic Group Metal Ions

Organic cofactor Organic cofactor Inorganic cofactor

Bind loosely and temporarily
to enzyme
Many coenzyme are obtain
from vitamin
Example: NAD (vitamin B)
Binds tightly and perman-
Attach temporarily to enzyme
ently to enzyme
Zn2+ (the cofactor for carbonic
Cytochrome oxidase has anhydrase),
prosthetic group heme. Cl- (the cofactor for salivary
amylase)
Example: Zn2+,Ca2+, Mg2+, K+,
Example: FAD Fe2+ and Na+, Cl-
To be continued…

ENZYME