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Enzymes

Cofactors are essential non-protein compounds or metallic ions that assist enzymes in catalyzing biochemical reactions, categorized into inorganic ions and organic molecules called coenzymes. Coenzymes can be further divided into prosthetic groups, which are permanently bound, and cosubstrates, which are transiently bound to proteins. The document also discusses the role of cofactors in enzyme kinetics and provides examples of enzyme complexes that require multiple cofactors for their activity.

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35 views10 pages

Enzymes

Cofactors are essential non-protein compounds or metallic ions that assist enzymes in catalyzing biochemical reactions, categorized into inorganic ions and organic molecules called coenzymes. Coenzymes can be further divided into prosthetic groups, which are permanently bound, and cosubstrates, which are transiently bound to proteins. The document also discusses the role of cofactors in enzyme kinetics and provides examples of enzyme complexes that require multiple cofactors for their activity.

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bipasha.phd
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We take content rights seriously. If you suspect this is your content, claim it here.
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A cofactor is a non-protein chemical compound or metallic ion that is required

for an enzyme's role as a catalyst (a catalyst is a substance that increases the


rate of a chemical reaction). Cofactors can be considered "helper molecules"
that assist in biochemical transformations. The rates at which these happen
are characterized in an area of study called enzyme kinetics. Cofactors
typically differ from ligands in that they often derive their function by
remaining bound. Cofactors can be divided into two types: inorganic ions and
complex organic molecules called coenzymes. Coenzymes are mostly derived
from vitamins and other organic essential nutrients in small amounts. (Note
that some scientists limit the use of the term "cofactor" for inorganic
substances; both types are included here.) Coenzymes are further divided into
two types. The first is called a "prosthetic group", which consists of a
coenzyme that is tightly (or even covalently) and permanently bound to a
protein. The second type of coenzymes are called "cosubstrates", and are
transiently bound to the protein. Cosubstrates may be released from a protein
at some point, and then rebind later. Both prosthetic groups and cosubstrates
have the same function, which is to facilitate the reaction of enzymes and
proteins. An inactive enzyme without the cofactor is called an apoenzyme,
while the complete enzyme with cofactor is called a holoenzyme. in each
enzymatic turnover.)
(Note that the International Union of Pure and Applied Chemistry (IUPAC) defines
"coenzyme" a little differently, namely as a low-molecular-weight, non-protein
organic compound that is loosely attached, participating in enzymatic reactions as
a dissociable carrier of chemical groups or electrons; a prosthetic group is defined
as a tightly bound, nonpolypeptide unit in a protein that is regenerated For
example, the multienzyme complex pyruvate dehydrogenase at the junction
of glycolysis and the citric acid cycle requires five organic cofactors and one metal
ion: loosely bound thiamine pyrophosphate (TPP), covalently
bound lipoamide and flavin adenine dinucleotide (FAD),
cosubstrates nicotinamide adenine dinucleotide

(NAD+) and coenzyme A (CoA), and a metal ion (Mg2+).Organic cofactors are
often vitamins or made from vitamins. Many contain the nucleotide adenosine
monophosphate (AMP) as part of their structures, such as ATP, coenzyme A, FAD,
and NAD+. This common structure may reflect a common evolutionary Some
enzymes or enzyme complexes require several cofactors. origin as part
of ribozymes in an ancient RNA world. It has been suggested that the AMP part of
the molecule can be considered to be a kind of "handle" by which the enzyme can
"grasp" the coenzyme to switch it between different catalytic centers.

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