Dimethylallylcistransferase

Dimethylallylcistransferase (DMAT) is an enzyme that plays a crucial role in the biosynthesis of terpenoids, a large and diverse class of naturally occurring organic chemicals. This enzyme is part of the mevalonate pathway, which is responsible for the production of isoprene units, the building blocks of terpenoids.

Function

Dimethylallylcistransferase catalyzes the transfer of a dimethylallyl group from dimethylallyl pyrophosphate (DMAPP) to isopentenyl pyrophosphate (IPP), resulting in the formation of geranyl pyrophosphate (GPP). This reaction is a key step in the biosynthesis of terpenoids.

Structure

The structure of dimethylallylcistransferase has been determined using X-ray crystallography. The enzyme is a monomer and consists of a single polypeptide chain. The active site of the enzyme, where the reaction takes place, is located in a deep pocket within the protein structure.

Clinical significance

Alterations in the activity of dimethylallylcistransferase can lead to abnormalities in the production of terpenoids, which can have various clinical implications. For example, reduced activity of this enzyme can lead to a deficiency in the production of cholesterol, a type of terpenoid that is essential for the formation of cell membranes and the synthesis of certain hormones.

See also

• Terpenoid
• Mevalonate pathway
• Isoprene
• Cholesterol

References

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