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

4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase
Identifiers
EC number	2.7.1.148
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, a 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase (EC 2.7.1.148) is an enzyme that catalyzes the chemical reaction

ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol $\rightleftharpoons$ ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol

Thus, the two substrates of this enzyme are ATP and 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol, whereas its two products are ADP and 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.

This enzyme belongs to the family of transferases, specifically those 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. This enzyme participates in biosynthesis of steroids.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1OJ4, 1UEK, 2V2Q, 2V2V, 2V2Z, 2V34, and 2V8P.

References

• Fellermeier M, Sagner S, Zenk MH, Bacher A, Eisenreich W (2000). "Biosynthesis of terpenoids: YchB protein of Escherichia coli phosphorylates the 2-hydroxy group of 4-diphosphocytidyl-2C-methyl-d-erythritol". Proc. Natl. Acad. Sci. U.S.A. 97 (3): 1062–7. doi:10.1073/pnas.97.3.1062. PMC 15522. PMID 10655484. 
• Seto H (2000). "Studies on the nonmevalonate pathway: conversion of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol to its 2-phospho derivative by 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase". Tetrahedron Lett. 41 (16): 2925–2928. doi:10.1016/S0040-4039(00)00295-1.