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Enzymes: A Protein With Catalytic Properties Due To Its Power of Specific Activation

Enzymes are proteins that catalyze chemical reactions without being consumed in the process. They do this by lowering the activation energy of reactions, creating a new reaction pathway. The active site of an enzyme is shaped specifically to bind to its substrate, and the substrate fits into the active site like a key fits into a lock. Factors like pH, temperature, and inhibitors can affect the functioning of enzymes by changing their structures.

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44 views

Enzymes: A Protein With Catalytic Properties Due To Its Power of Specific Activation

Enzymes are proteins that catalyze chemical reactions without being consumed in the process. They do this by lowering the activation energy of reactions, creating a new reaction pathway. The active site of an enzyme is shaped specifically to bind to its substrate, and the substrate fits into the active site like a key fits into a lock. Factors like pH, temperature, and inhibitors can affect the functioning of enzymes by changing their structures.

Uploaded by

Ash-shirHasan
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PPT, PDF, TXT or read online on Scribd
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ENZYMES

A protein with catalytic properties due to its


power of specific activation
Chemical reactions

Chemical reactions need an initial input of energy =


THE ACTIVATION ENERGY

During this part of the reaction the molecules are


said to be in a transition state.
Reaction pathway
Main! reactions !o "aster

Increasing the temperature make molecules move


faster

Biological systems are very sensitive to temperature


changes.

Enzymes can increase the rate of reactions without


increasing the temperature.

hey do this by lowering the activation energy.

hey create a new reaction pathway !a short cut"


An en#yme controlle$ pathway

Enzyme controlled reactions proceed #$% to #$## times faster


than corresponding non&enzymic reactions.
En#yme str%ct%re

Enzymes are
proteins

hey have a
!lo&%lar shape

' comple( '()


structure
H%man pancreatic amylase

The acti*e site

)ne part of an enzyme*


the active site* is
particularly important

he shape and the


chemical en*ironment
inside the active site
permits a chemical
reaction to proceed
more easily
Co"actors

'n additional non&


protein molecule that is
needed by some
enzymes to help the
reaction

ightly bound cofactors


are called prosthetic
groups

Cofactors that are bound


and released easily are
called coenzymes

+any vitamins are


coenzymes
Nitrogenase enzyme with Fe, Mo and ADP cofactors
The s%&strate

he substrate of an enzyme are the reactants


that are activated by the enzyme

Enzymes are speci"ic to their substrates

he specificity is determined by the acti*e


site
The +oc an$ ,ey Hypothesis

,it between the substrate and the active site of the enzyme is
e(act

-ike a key fits into a lock very precisely

he key is analogous to the enzyme and the substrate


analogous to the lock.

emporary structure called the enzyme&substrate comple(


formed

.roducts have a different shape from the substrate

)nce formed* they are released from the active site

-eaving it free to become attached to another substrate


The +oc an$ ,ey Hypothesis
Enzyme may
be used again
Enzyme-
substrate
complex
E
S
P
E
E
P
Reaction coordinate
The +oc an$ ,ey Hypothesis

his e(plains enzyme specificity

his e(plains the loss of activity when


enzymes denature
The In$%ce$ -it Hypothesis

/ome proteins can change their shape


0conformation1

2hen a substrate combines with an enzyme* it


induces a change in the enzyme3s conformation

he active site is then moulded into a precise


conformation

+aking the chemical environment suitable for the


reaction

he bonds of the substrate are stretched to make the


reaction easier 0lowers activation energy1
The In$%ce$ -it Hypothesis

his e(plains the enzymes that can react with a


range of substrates of similar types
4e(okinase 0a1 without 0b1 with glucose substrate
http566www.biochem.arizona.edu6classes6bioc7896789a6:)E/6E:;<+E/6enzyme=mechanism.html
-actors a""ectin! En#ymes

substrate concentration

p4

temperature

inhibitors
S%&strate concentration. Non(en#ymic reactions

he increase in velocity is proportional to the


substrate concentration
Reaction
velocity
Substrate concentration
S%&strate concentration. En#ymic reactions

,aster reaction but it reaches a saturation point when all the


enzyme molecules are occupied.

If you alter the concentration of the en#yme then V


ma/
will
change too.
Reaction
velocity
Substrate concentration
V
max
The e""ect o" pH
Optimum pH values
Enzyme
activity
Trypsin
Pepsin
pH
1
!
" # 11
The e""ect o" pH

E(treme p4 levels will produce $enat%ration

he structure of the enzyme is changed

he active site is distorted and the substrate


molecules will no longer fit in it

't p4 values slightly different from the enzyme3s


optimum value* small changes in the charges of the
enzyme and it3s substrate molecules will occur

his change in ionisation will affect the binding of


the substrate with the active site.
The e""ect o" temperat%re

>#$ 0the temperat%re coe""icient1 = the increase in


reaction rate with a #$?C rise in temperature.

,or chemical reactions the >#$ = 9 to @


0the rate of the reaction doubles or triples with every
#$?C rise in temperature1

Enzyme&controlled reactions follow this rule as they


are chemical reactions

BA at high temperatures proteins $enat%re

he optimum temperature for an enzyme controlled


reaction will be a balance between the >#$ and
denaturation.
The e""ect o" temperat%re
Temperature $ %&
Enzyme
activity
'
1'
(' ' )' !'
*1'
+enaturation
The e""ect o" temperat%re

,or most enzymes the optimum temperature is about


@$?C

+any are a lot lower*


cold water fish will die at @$?C because their
enzymes denature

' few bacteria have enzymes that can withstand very


high temperatures up to #$$?C

+ost enzymes however are fully denatured at B$?C


Inhi&itors

Inhibitors are chemicals that reduce the rate of


enzymic reactions.

he are usually specific and they work at low


concentrations.

hey block the enzyme but they do not


usually destroy it.

+any drugs and poisons are inhibitors of


enzymes in the nervous system.
The e""ect o" en#yme inhi&ition

Irre*ersi&le inhi&itors. Combine with the


functional groups of the amino acids in the
active site* irreversibly.
E/amples. nerve gases and pesticides*
containing organophosphorus* combine with
serine residues in the enzyme acetylcholine
esterase.
The e""ect o" en#yme inhi&ition

Re*ersi&le inhi&itors. hese can be washed


out of the solution of enzyme by dialysis.
here are two categories.
The e""ect o" en#yme inhi&ition
01 Competiti*e. hese
compete with the
substrate molecules for
the active site.
he inhibitor3s action is
proportional to its
concentration.
Cesembles the substrate3s
structure closely.
Enzyme inhibitor
comple
!eversible
reaction
E " #
E#
The e""ect o" en#yme inhi&ition
S%ccinate -%marate 2 3H
2
2 3e
(
Succinate dehydrogenase
CH
3
COOH
CH
3
COOH CHCOOH
CHCOOH
COOH
COOH
CH
3
,alonate
The e""ect o" en#yme inhi&ition
31 Non(competiti*e. hese are not influenced by the
concentration of the substrate. It inhibits by binding
irreversibly to the enzyme but not at the acti*e site1
E/amples

Cyanide combines with the Iron in the enzymes


cytochrome o(idase.

4eavy metals* A! or H!* combine with 4SH groups.


hese can be removed by using a chelating agent such
as ED'.
Applications o" inhi&itors

Ne!ati*e "ee$&ac5 end point or end product


inhibition

5oisons snake bite* plant alkaloids and nerve


gases.

Me$icine antibiotics* sulphonamides*


sedatives and stimulants

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