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

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4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase
Identifiers
EC no. 2.7.1.148
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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-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate ADP + 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate

Thus, the two substrates of this enzyme are ATP and 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME), whereas its two products are ADP and 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-MEP).

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, and IspE. This enzyme participates in the MEP pathway (non-mevalonate pathway) of isoprenoid precursor biosynthesis.

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.

Related Research Articles

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2-<i>C</i>-Methylerythritol 4-phosphate Chemical compound

2-C-Methyl-D-erythritol 4-phosphate (MEP) is an intermediate on the MEP pathway of isoprenoid precursor biosynthesis. It is the first committed metabolite on that pathway on the route to IPP and DMAPP.

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4-Diphosphocytidyl-2-C-methylerythritol is an intermediate in the MEP pathway of isoprenoid precursor biosynthesis. It is produced by the enzyme 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) and is a substrate for CDP-ME kinase (IspE).

4-Diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate is an intermediate in the MEP pathway of isoprenoid precursor biosynthesis.

<span class="mw-page-title-main">YgbB N terminal protein domain</span>

In molecular biology, YgbB is a protein domain. This entry makes reference to a number of proteins from eukaryotes and prokaryotes which share this common N-terminal signature and appear to be involved in terpenoid biosynthesis. The YgbB protein is a putative enzyme thought to aid terpenoid and isoprenoid biosynthesis, a vital chemical in all living organisms. This protein domain is part of an enzyme which catalyses a reaction in a complex pathway.

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References