2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
| 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.6.1.12 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
2-C-Methyl-D-erythritol 2,4-cyclodiphosphate synthase (MEcPP synthase, IspF, EC 4.6.1.12) is a zinc-dependent enzyme and a member of the YgbB N terminal protein domain, which participates in the MEP pathway (non-mevalonate pathway) of isoprenoid precursor biosynthesis. It catalyzes the following reaction:[1]
- 4-diphosphocytidyl-2-C-methyl-D)erythritol 2-phosphate 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP
The enzyme is considered a phosphorus-oxygen lyase. The systematic name of this enzyme class is 2-phospho-4-(cytidine 5′-diphospho)-2-C-methyl-D-D-erythritol CMP-lyase (cyclizing; 2-C-methyl-D-erythritol 2,4-cyclodiphosphate-forming). Other names in common use include IspF, YgbB and MEcPP synthase.
Structural studies
[edit]As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes 1GX1, 1H47, 1H48, 1IV1, 1IV2, 1IV3, 1IV4, 1T0A, 1U3L, 1U3P, 1U40, 1U43, 1VH8, 1VHA, 1W55, 1W57, 1YQN, 2AMT, 2GZL, and 2PMP.
References
[edit]- ^ Herz S, Wungsintaweekul J, Schuhr CA, Hecht S, Lüttgen H, Sagner S, Fellermeier M, Eisenreich W, Zenk MH, Bacher A, Rohdich F (2000). "Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-d-erythritol 2-phosphate to 2C-methyl-d-erythritol 2,4-cyclodiphosphate". Proc. Natl. Acad. Sci. USA. 97 (6): 2486–90. Bibcode:2000PNAS...97.2486H. doi:10.1073/pnas.040554697. PMC 15955. PMID 10694574.
