4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase

4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase () is an enzyme that catalyzes the chemical reaction

The enzyme characterised from Escherichia coli converts 4-diphosphocytidyl-2-C-methylerythritol (CDP-ME) to its 2-phosphate derivative, 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-MEP) by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The reaction is part of the non-mevalonate pathway to terpenes.

This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol 2-phosphotransferase. This enzyme is also called CDP-ME kinase, and IspE.

Structural studies As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .

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