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Cofactors, Coenzymes, and Prosthetic Groups

Cofactors are non-protein chemical compounds or metallic ions required for an enzyme's activity that assist in biochemical transformations. Cofactors can be inorganic ions or complex organic coenzymes derived from vitamins. Enzymes require cofactors to be active; inactive enzymes lacking cofactors are called apoenzymes, while active enzymes with cofactors are called holoenzymes. Some enzymes require several different cofactors, both organic and inorganic, like the pyruvate dehydrogenase enzyme complex. Organic cofactors are often made from vitamins and contain adenosine monophosphate, reflecting a potential common evolutionary origin.

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126 views1 page

Cofactors, Coenzymes, and Prosthetic Groups

Cofactors are non-protein chemical compounds or metallic ions required for an enzyme's activity that assist in biochemical transformations. Cofactors can be inorganic ions or complex organic coenzymes derived from vitamins. Enzymes require cofactors to be active; inactive enzymes lacking cofactors are called apoenzymes, while active enzymes with cofactors are called holoenzymes. Some enzymes require several different cofactors, both organic and inorganic, like the pyruvate dehydrogenase enzyme complex. Organic cofactors are often made from vitamins and contain adenosine monophosphate, reflecting a potential common evolutionary origin.

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A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's

activity. Cofactors can be considered "helper molecules" that assist in biochemical


transformations. The rates at which these happen are characterized by enzyme kinetics.

Cofactors can be subclassified as either inorganic ions or complex organic molecules called
coenzymes,[1] the latter of which is mostly derived from vitamins and other organic essential
nutrients in small amounts. A coenzyme that is tightly or even covalently bound is termed a
prosthetic group.[2] Cosubstrates are transiently bound to the protein and will be released at
some point, then get back in. The prosthetic groups, on the other hand, are bound permanently to
the protein. Both of them have the same function, which is to facilitate the reaction of enzymes
and protein. Additionally, some sources also limit the use of the term "cofactor" to inorganic
substances.[3][4] An inactive enzyme without the cofactor is called an apoenzyme, while the
complete enzyme with cofactor is called a holoenzyme.[5]

Some enzymes or enzyme complexes require several cofactors. For example, the multienzyme
complex pyruvate dehydrogenase[6] 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), and the cosubstrates
nicotinamide adenine dinucleotide (NAD+) and coenzyme A (CoA), and a metal ion (Mg2+).[7]

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 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.[8]

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