IPR020555
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, conserved site
InterPro entry
Short name | MECDP_synthase_CS |
Description
IspF is a MECDP (2-C-methyl-D-erythritol 2,4-cyclodiphosphate) synthetase, also known as YgbB. It is an enzyme in the non-mevalonate pathway of isoprenoid synthesis. Isoprenoids are essential in all organisms, and can also be synthesized through the mevalonate pathway. The non-mevolante route is used by many bacteria and human pathogens, including Mycobacterium tuberculosis and Plasmodium falciparum. This route appears to involve seven enzymes. MECDP synthetase catalyses the intramolecular attack by a phosphate group on a diphosphate, with cytidine monophosphate (CMP) acting as the leaving group to give the cyclic diphosphate product MEDCP. The enzyme is a trimer with three active sites shared between adjacent copies of the protein. The enzyme also has two metal binding sites, the metals playing key roles in catalysis
[1].
A number of proteins from eukaryotes and prokaryotes are bifunctional proteins with an N-terminal IspD domain and a C-terminal IspF domain
[2].
This entry represents a MECDP (2-C-methyl-D-erythritol 2,4-cyclodiphosphate) synthetase conserved site.
References
1.Structure and catalytic mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) synthase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis. Kishida H, Wada T, Unzai S, Kuzuyama T, Takagi M, Terada T, Shirouzu M, Yokoyama S, Tame JR, Park SY. Acta Crystallogr. D Biol. Crystallogr. 59, 23-31, (2003). PMID: 12499535
2.Biosynthesis of isoprenoids: a bifunctional IspDF enzyme from Campylobacter jejuni. Gabrielsen M, Rohdich F, Eisenreich W, Grawert T, Hecht S, Bacher A, Hunter WN. Eur. J. Biochem. 271, 3028-35, (2004). View articlePMID: 15233799
GO terms
biological process
- None
cellular component
- None
Cross References
Contributing Member Database Entry
- PROSITE patterns:PS01350