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(1)

ENZYMES

ENZYMES

Department

(2)

 EnzymesEnzymes areare biological catalystsbiological catalysts iin living organisms, .n living organisms, . 

 They increase the speed of the reactionsThey increase the speed of the reactions byby decreasingdecreasing the

the activationactivation energyenergy. . 

 TheyThey dondon’’tt effecteffect rreaction equilibrium constantseaction equilibrium constants andand thermodinamics

thermodinamics of of thethe reactionreaction.. 

 All enzymes are protein structures except a small group All enzymes are protein structures except a small group of catalytic RNA molecules

of catalytic RNA molecules calledcalled ribozymesribozymes.. 

 TheyThey exhibitexhibit differentdifferent formsforms of of specifityspecifity ((absoluteabsolute specifity

specifity, , boundbound specifityspecifity, , stereochemicalstereochemical specifityspecifity, , groupgroup specifity

specifity).). 

 TheyThey can can stillstill havehave activityactivity afterafter isolationisolation fromfrom biologicalbiological milieu

milieu.. 

 TheirTheir MWsMWs rangerange betweenbetween 1000010000--2000000.2000000. 

 TheyThey increaseincrease thethe rate of rate of reactionsreactions moremore thanthan 101099 foldfold..

(3)

•Activation energy

•Stabilization of the transition state

•Free energy change (ΔG-Free Gibbs Energy change of

the reaction)

(4)

The molecules upon which enzymes may act are called

substrates. Enzymes bind to their substrates from a special region called active site.

A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme’s biological activity. Organic cofactors are usually made from vitamins and called coenzymes. In some cases, both coenzymes and cofactors are required for the activity. A catalytically active enzyme consisting of an apoenzyme combined with its cofactor is called holoenzyme. The protein part of an enzyme without the cofactor is called apoenzyme. Enzymes that differ in amino acid sequence but catalyze the same reaction are called isozymes (isoenzymes).

(5)

A coenzyme that is tightly or even covalently bound is called a prosthetic group. Flavins, Heme group in cytochrome c and biotin are examples of a prosthetic group.

(6)

• Lock and key model →→ The fit between the substrate

and active site of the enzyme is very specific like that of

a lock and key.

•Induced fit model →→ The active site of the enzyme

may change in order to fit the substrate molecule.

(7)

SPECIFITY OF ENZYMES

•Enzymes are highly specific biocatalysts that

can only interact with one or several

substrates and catalyze only one type of

reaction.

(8)

Classification

Classification

of

of

Enzymes

Enzymes

An enzyme has two names. The first one is the

recommended name for daily use. The second is the more systematic full name that is used when the

enzyme is to be identified in case of uncertainty.

1. Recommended name: Generally, the names of the

most commonly used enzymes are obtained by adding a suffix (such as urease, glucosidase) to the end of the substrate used in that reaction. However, there are

also enzyme names (pepsin, trypsin, etc.) that do not give an idea about the reaction they catalyze.

2. Systematic name: According to this nomenclature, enzymes are divided into 6 classes.

(9)

International Union of Biochemistry and

Molecular Biology (IUBMB) suggested a

classification for enzymes which classify

enzymes in 6 main groups.

Classification

(10)

1

1

-

-

Oxidoreductases

Oxidoreductases

:

:

They

They

catalyze the transfer

catalyze the transfer

of hydrogen or oxygen

of hydrogen or oxygen

atoms

atoms

Classification

Classification

of

of

Enzymes

Enzymes

Dehydrogenases

Dehydrogenases

Oxidases

Oxidases

Reductases

Reductases

Peroxidases

Peroxidases

Catalase

Catalase

Oxygenases

Oxygenases

Hydroxylases

Hydroxylases

(11)

2

2

-

-

Transferases

Transferases

They

They

catalyse

catalyse

the

the

transfer of

transfer of

groups

groups

having

having

C

C

-

-

, N

, N

-

-

or

or

P

P

-

-

groups

groups

.

.

Transaldolase

Transaldolase

and

and

transketolase

transketolase

Acyl

Acyl

,

,

methyl

methyl

,

,

glucosyl

glucosyl

ve

ve

phosphoryl

phosphoryl

transferases

transferases

Kinases

Kinases

Phosphomutases

Phosphomutases

Classification

(12)

3

3

-

-

Hydrolases

Hydrolases

They

They

catalyse

catalyse

the

the

hydrolytic

hydrolytic

cleavage

cleavage

of

of

bonds

bonds

.

.

Esterases

Esterases

Glucosidases

Glucosidases

Peptidases

Peptidases

Phosphatases

Phosphatases

Tyolases

Tyolases

Phospholipases

Phospholipases

Amidases

Amidases

Deaminases

Deaminases

Ribonucleases

Ribonucleases

Classification

(13)

4

4

-

-

Lyases

Lyases

They

They

catalyse

catalyse

the

the

cleavage

cleavage

of C

of C

-

-

C, C

C, C

-

-

S ve

S ve

C

C

-

-

N

N

bonds

bonds

.

.

Decarboxylases

Decarboxylases

Aldolases

Aldolases

Hydratases

Hydratases

Dehydratases

Dehydratases

Synthases

Synthases

Lyases

Lyases

Classification

(14)

5

5

-

-

Isomerases

Isomerases

They

They

catalyse

catalyse

the

the

rasemization

rasemization

reactions

reactions

of

of

optical

optical

or

or

geometrical

geometrical

isomers.

isomers

.

Rasemases

Rasemases

Epimerases

Epimerases

İ

İ

zomerases

zomerases

Mutases

Mutases

Classification

(15)

6

6

-

-

Lygases

Lygases

T

T

hey

hey

catalyse

catalyse

formation

formation

of

of

bonds

bonds

between

between

C

C

and

and

O, S,

O, S,

N

N

coupled

coupled

to

to

ATP

ATP

and

and

GTP

GTP

hydrolysis

hydrolysis

.

.

Synthethases

Synthethases

Carboxylases

Carboxylases

Classification

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