Function
MECDP synthase (MECPS) participates in mevalonate-independent steroid biosynthesis. It converts 2-phospho-4-(cytidine 5’-diphospho)-2-C-methyl-D-erythritol (2P-CDME) to 2-C-methyl-D-erythritol 2, 4-cyclodiphosphate (MECP) and CMP. MECPS contains metal binding sites which are required for catalysis[1].
Relevance
MECPS is a potential antimalarial drug target[2].
Structural highlights
MECPS active site is located in a cleft between 2 subunits and contains the metal ions[3]. Water molecules are shown as red spheres.
- ↑ Richard SB, Ferrer JL, Bowman ME, Lillo AM, Tetzlaff CN, Cane DE, Noel JP. Structure and mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase. An enzyme in the mevalonate-independent isoprenoid biosynthetic pathway. J Biol Chem. 2002 Mar 8;277(10):8667-72. Epub 2002 Jan 10. PMID:11786530 doi:https://dx.doi.org/10.1074/jbc.C100739200
- ↑ Kishida H, Wada T, Unzai S, Kuzuyama T, Takagi M, Terada T, Shirouzu M, Yokoyama S, Tame JR, Park SY. 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. Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):23-31. Epub 2002, Dec 19. PMID:12499535
- ↑ Kemp LE, Bond CS, Hunter WN. Structure of 2C-methyl-D-erythritol 2,4- cyclodiphosphate synthase: an essential enzyme for isoprenoid biosynthesis and target for antimicrobial drug development. Proc Natl Acad Sci U S A. 2002 May 14;99(10):6591-6. Epub 2002 May 7. PMID:11997478 doi:10.1073/pnas.102679799
