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Enzyme Cofactors and Inhibitors

Enzymes require cofactors to function properly. There are two main types of cofactors - prosthetic groups which are permanently bound to enzymes, and coenzymes which temporarily bind and transfer chemical groups. Some enzymes exist as inactive precursors until a cofactor binds and induces a conformational change activating the enzyme. Enzyme inhibitors interfere with enzyme activity and can be competitive, non-competitive, reversible or irreversible. The final product of a metabolic pathway often inhibits an earlier enzyme as a feedback mechanism to regulate pathway activity.

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24 views4 pages

Enzyme Cofactors and Inhibitors

Enzymes require cofactors to function properly. There are two main types of cofactors - prosthetic groups which are permanently bound to enzymes, and coenzymes which temporarily bind and transfer chemical groups. Some enzymes exist as inactive precursors until a cofactor binds and induces a conformational change activating the enzyme. Enzyme inhibitors interfere with enzyme activity and can be competitive, non-competitive, reversible or irreversible. The final product of a metabolic pathway often inhibits an earlier enzyme as a feedback mechanism to regulate pathway activity.

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layet39267
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Enzyme Cofactors and Inhibitors

 Some enzymes need a cofactor before they can catalyse a reaction


Cofactor: non-protein substance
Two main types of cofactor:
Prosthetic group: inorganic groups that are permanently bound to the enzyme
e.g. iron, zinc, copper
Coenzymes: organic molecules that bind only temporarily to the enzyme,
transferring a chemical group necessary required for the reaction e.g. Vit C &
ATP
Enzyme Cofactors:
 Some enzymes require cofactors to be active
 Cofactors may be permanently attached so are prosthetic groups or
temporarily attached coenzymes which detach after a reaction and may
participate with another enzyme in other reactions

Precursor Activation:
 Some enzymes are too damaging to have in an active form in the cell
 Such enzymes usually exist in an inactive form that will only function if
a cofactor is present
 The cofactor changes the shape of an active site so that it is now
complementary and will function
 Inactive precursor without cofactor= apoenzyme
 Activated precursor with co-factor attached=holoenzyme
Other ways to activate enzymes:
 By the action of another enzyme, which cleaves (breaks) certain bonds in
the molecule
 Certain conditions e.g. change in pH or temp will change tertiary
structure and make it active – called zymogens or proenzymes
 Pepsin – secreting active pepsin would damage the cells in stomach so a
proenzyme pepsinogen is released and the low pH activates it
 E.g. blood clotting (is an important biological response to tissue damage.
Begins when platelets aggregate at the site of tissue damage and the
aggregated platelets release clotting factors including factor X. Factor X
depends on the cofactor Vit K for activation, Activated factor X catalyses
the conversion prothrombin into the enzyme thrombin by cleaving certain
bonds in the molecule so its tertiary structure is altered. Thrombin
catalyses the conversion of soluble fibrinogen to insoluble fibrin fibres
and fibrin molecules together with platelets form a blood clot
Enzyme inhibitors:
 Inhibitors are substances that can interfere with enzyme activity, they can
be:
o Competitive or noncompetitive depending on whether they
compete with the substrate for binding at the active site or not
 Can be reversible or irreversible depending on whether their inhibitory
effect on the enzyme is permanent or not
 Competitive inhibition: Inhibitors usually have a shape that closely
resembles that of the enzymes normal substrate molecule, the competitive
inhibitor binds to the active site creating an enzyme inhibitor complex
and blocking the substrate molecule which prevents the normal reaction
 Reversible inhibitors bind to active site with weak hydrogen bonds which
are broken easily
 Non competitive: Have a completely different shape to the normal
substrate molecule as they don’t bind to the active site, instead they bind
to an allosteric site
 If the inhibitor is a reversible inhibitor, it can dissociate from the
allosteric site which causes the active site to revert to its normal size and
the substrate can bind as normal
Graph on rate of reaction with non competitive inhibitor
Examples of Competitive Inhibitors:
 Statins – reduce cholesterol, are competitive inhibitors of an enzyme used
to synthesize cholesterol’
 Aspirin – Irreversibly inhibits COX enzymes which prevent the synthesis
of chemicals responsible for producing pain and fever
Examples of non-competitive inhibitors:
 Organophosphates- chemicals used as pesticides, they irreversibly inhibit
the enzyme acetylcholinesterase, which is needed for nerve conduction at
synapses
 Cyanide is an irreversible inhibitor of an enzyme involved in respiration
End- product inhibition:
 Enzyme inhibition is important in regulating metabolic pathways, The
final (end) product often acts as a regulator of the pathway in a process
called end-product inhibition
 When the amount of product is high, it binds non-competitively to an
enzyme in the pathway, blocking further production of itself
 When the amount of end product falls, inhibition ends and the pathway
restarts
 The synthesis of ATP is regulated in this way, with ATP acting as the
inhibitor

Example:
 During the first part of respiration, glucose has 2 phosphate groups
added to it.
 The addition of the second phosphate group is catalysed by an enzyme
phosphofructokinase (PFK).
 This enzyme is competitively inhibited by ATP, which is produced
during respiration.
 When ATP is high, ATP competes for the PFK active site, preventing
the addition of the second phosphate group to glucose, and so
eventually reducing the production of ATP
 If ATP levels then fall, the PFK enzyme is no longer inhibited, glucose
has the second phosphate added and ATP will be produced again.

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