Isopentenyl phosphate kinase () is an enzyme with systematic name ATP:isopentenyl phosphate phosphotransferase. It catalyses the following chemical reaction
The enzyme first characterised from peppermint and Escherichia coli converts isopentenyl phosphate to isopentenyl pyrophosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).
This enzyme takes part in a modified mevalonate pathway in Archaea such as Methanocaldococcus jannaschii. Its structure has been determined by X-ray crystallography.
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