2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
| 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.7.60 | ||||||||
| CAS number | Template:CAS | ||||||||
| 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 | ||||||||
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| IspD | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| File:PDB 1w77 EBI.jpg
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) from Arabidopsis thaliana
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| Identifiers | |||||||||
| Symbol | IspD | ||||||||
| Pfam | PF01128 | ||||||||
| Pfam clan | CL0110 | ||||||||
| InterPro | IPR001228 | ||||||||
| PROSITE | PDOC00997 | ||||||||
| SCOP | 1inj | ||||||||
| SUPERFAMILY | 1inj | ||||||||
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In enzymology, a 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60) is an enzyme that catalyzes the chemical reaction:
- 2-C-methyl-D-erythritol 4-phosphate + CTP
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Thus, the two substrates of this enzyme are CTP and 2-C-methyl-D-erythritol 4-phosphate, whereas its two products are diphosphate and 4-diphosphocytidyl-2-C-methylerythritol.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases).
This enzyme participates in isoprenoid biosynthesis and stenvenosim. It catalyzes the third step of the MEP pathway; the formation of CDP-ME (4-diphosphocytidyl-2C-methyl-D-erythritol) from CTP and MEP (2C-methyl-D-erythritol 4-phosphate).[1] The isoprenoid pathway is a well known target for anti-infective drug development.[2][3]
Nomenclature
The systematic name of this enzyme class is CTP:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase. This enzyme is also called:
- MEP cytidylyltransferase
- CDP-ME synthetase
It is normally abbreviated IspD. It is also referenced by the open reading frame YgbP.
Structural studies
The crystal structure of the E. coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase 1I52, 1INI & 1INJ, reported by Richard et al. (2001), was the first one for an enzyme involved in the MEP pathway.
As of February 2010, 13 other structures have been solved for this class of enzymes, with PDB accession codes 1H3M, 1VGT, 1VGU, 1VGZ, 1VPA, 1VGW, 1W55, 1W57, 1W77,2PX7, 2VSI, 3F1C and 2VSH.
References
Further reading
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This article incorporates text from the public domain Pfam and InterPro IPR001228
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