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The document discusses the roles and characteristics of cofactors and coenzymes in biochemical reactions, highlighting that cofactors are necessary for enzyme activity and can be organic or inorganic. Coenzymes, a subset of cofactors, are low-molecular weight organic substances that assist in transporting groups between enzymes and are often related to vitamins. It also outlines environmental factors affecting enzyme action, including temperature, pH, and concentrations of enzymes and substrates.

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0% found this document useful (0 votes)
11 views3 pages

Notes Extension

The document discusses the roles and characteristics of cofactors and coenzymes in biochemical reactions, highlighting that cofactors are necessary for enzyme activity and can be organic or inorganic. Coenzymes, a subset of cofactors, are low-molecular weight organic substances that assist in transporting groups between enzymes and are often related to vitamins. It also outlines environmental factors affecting enzyme action, including temperature, pH, and concentrations of enzymes and substrates.

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dethyoke
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Isaac O.

Obonyo lectures@2025

Cofactors and Coenzymes


A. Co-factor
 A cofactor is a non-protein chemical compound that is required for the protein's
biological activity. Cofactors can be considered "helper molecules" that assist in
biochemical transformations.
 Cofactors can be divided into two broad groups: organic cofactors, such as ATP,
NAD+ and inorganic cofactors, such as the metal ions Mg2+, Cu+, Mn2+
 Organic cofactors are small organic molecules that can be either loosely or tightly
bound to the enzyme and directly participate in the reaction.
 Loosely bound cofactors are termed as coenzymes.

B. Coenzymes
Features of coenzyme
i. Coenzymes are heat stable.
ii. They are low-molecular weight substances.
iii. The coenzymes combine loosely with the enzyme molecules and so, the
coenzyme can be separated easily. When the reaction is completed, the coenzyme
is released from the apo-enzyme, and goes to some other reaction site. An
apoenzyme is an inactive enzyme, activation of the enzyme occurs upon binding
of an organic or inorganic cofactor. Holoenzyme- An apoenzyme together with
its cofactor. A holoenzyme is complete and catalytically active.
iv. Coenzymes which are directly involved and altered in the course of chemical
reactions are considered to be a type of secondary substrate.
v. Many coenzymes are closely related to vitamins. Some of them are important
growth factors are the precursors of vitamins.

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Isaac O. Obonyo lectures@2025

Role of coenzyme
1. The function of coenzymes is to transport groups between enzymes.
 Coenzymes in Hydrogen transfer reaction: These coenzymes involved in
hydrogen transfer reaction and form essential components of dehydrogenase.
These NAD+ and NADP are coenzymes of a number of dehydrogenases catalyzing
oxidation-reduction reaction.
 Coenzymes involved in group transfer: e.g., biotin is a coenzyme belonging to
vitamin B group which is an essential growth factor for yeast and other
microorganism. Biotin is a water-soluble vitamin and participate in transfer of
carboxyl group.
 Coenzymes which loss or gain these chemical groups in the course of the reaction
are often reformed in the same metabolic pathway. For example, NAD + used in
glycolysis and the citric acid cycle is replaced in the electron transport chain.
 Other: Phosphate groups which are carried by coenzymes such as ATP, Acetyl
groups which are carried by coenzymes such as coenzyme A.
2. The coenzyme is essential for the biological activity of the enzyme.
 A coenzyme is a low molecular weight organic substance, without which the
enzyme cannot exhibit any reaction. One molecule of the coenzyme is able to
convert a large number of substrate molecules with the help of enzyme.
 Important coenzyme Alcohol dehydrogenase Coenzyme A  Flavin adenine
dinucleotide (FAD) Nicotinamide adenine dinucleotide (NAD) Adenosine
triphosphate (ATP)

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Isaac O. Obonyo lectures@2025

Environmental condition affecting action of enzymes


1. Temperature: Raising temperature generally speeds up a reaction, and lowering
temperature slows down a reaction. However, extreme high temperatures can
cause an enzyme to lose its shape (denature) and stop working.
2. pH: Each enzyme has an optimum pH range. Changing the pH outside of this
range will slow enzyme activity. Extreme pH values can cause enzymes to
denature.
3. Enzyme concentration: Increasing enzyme concentration will speed up the
reaction, as long as there is substrate available to bind to. Once all of the substrate
is bound, the reaction will no longer speed up, since there will be nothing for
additional enzymes to bind to.
4. Substrate concentration: Increasing substrate concentration also increases the
rate of reaction to a certain point. Once all of the enzymes have bound, any
substrate increase will have no effect on the rate of reaction, as the available
enzymes will be saturated and working at their maximum rate.

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