MEP cytidylyltransferase

Function

MEP cytidylyltransferase (MEPCT) catalyzes the conversion of 2C-methyl-D-erythritol 4-phosphate and CTP to 4-(cytidine 5’-diphospho)- 2C-methyl-D-erythritol (CDP-ME) and diphosphate. MEPCT participates in isoprenoid biosynthesis in many bacteria while eukaryotes use the mevalonic acid pathway for the isoprenoed biosynthesis^[1]. IspD/IspDF is a bifunctional enzyme which catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erithritol 4-phophate and the conversion or CDP-ME2P to ME-CPP^[2].

Relevance

Inhibitors of MEPCT can be used as potential antibiotics^[3].

Structural highlights

The biological assembly of E. coli MEPCT is . The ^[4]. Water molecules shown as red spheres. .

3D structures of MEP cytidylyltransferase

MEP cytidylyltransferase 3D structures

Structure of E. coli MEP cytidylyltransferase complex with CTP, Mg+2 (small light green) and Ca+2 (large green) (PDB code 1i52).

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Friedrich R, Fuentes-Prior P, Ong E, Coombs G, Hunter M, Oehler R, Pierson D, Gonzalez R, Huber R, Bode W, Madison EL. Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase. J Biol Chem. 2002 Jan 18;277(3):2160-8. Epub 2001 Nov 5. PMID:11696548 doi:10.1074/jbc.M109830200
↑ Gabrielsen M, Rohdich F, Eisenreich W, Grawert T, Hecht S, Bacher A, Hunter WN. Biosynthesis of isoprenoids: a bifunctional IspDF enzyme from Campylobacter jejuni. Eur J Biochem. 2004 Jul;271(14):3028-35. doi: 10.1111/j.1432-1033.2004.04234.x. PMID:15233799 doi:http://dx.doi.org/10.1111/j.1432-1033.2004.04234.x
↑ Tsang A, Seidle H, Jawaid S, Zhou W, Smith C, Couch RD. Francisella tularensis 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase: kinetic characterization and phosphoregulation. PLoS One. 2011;6(6):e20884. doi: 10.1371/journal.pone.0020884. Epub 2011 Jun 9. PMID:21694781 doi:http://dx.doi.org/10.1371/journal.pone.0020884
↑ Richard SB, Bowman ME, Kwiatkowski W, Kang I, Chow C, Lillo AM, Cane DE, Noel JP. Structure of 4-diphosphocytidyl-2-C- methylerythritol synthetase involved in mevalonate- independent isoprenoid biosynthesis. Nat Struct Biol. 2001 Jul;8(7):641-8. PMID:11427897 doi:10.1038/89691

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] Friedrich R, Fuentes-Prior P, Ong E, Coombs G, Hunter M, Oehler R, Pierson D, Gonzalez R, Huber R, Bode W, Madison EL. Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase. J Biol Chem. 2002 Jan 18;277(3):2160-8. Epub 2001 Nov 5. PMID:11696548 doi:10.1074/jbc.M109830200

[2] Gabrielsen M, Rohdich F, Eisenreich W, Grawert T, Hecht S, Bacher A, Hunter WN. Biosynthesis of isoprenoids: a bifunctional IspDF enzyme from Campylobacter jejuni. Eur J Biochem. 2004 Jul;271(14):3028-35. doi: 10.1111/j.1432-1033.2004.04234.x. PMID:15233799 doi:http://dx.doi.org/10.1111/j.1432-1033.2004.04234.x

[3] Tsang A, Seidle H, Jawaid S, Zhou W, Smith C, Couch RD. Francisella tularensis 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase: kinetic characterization and phosphoregulation. PLoS One. 2011;6(6):e20884. doi: 10.1371/journal.pone.0020884. Epub 2011 Jun 9. PMID:21694781 doi:http://dx.doi.org/10.1371/journal.pone.0020884

[4] Richard SB, Bowman ME, Kwiatkowski W, Kang I, Chow C, Lillo AM, Cane DE, Noel JP. Structure of 4-diphosphocytidyl-2-C- methylerythritol synthetase involved in mevalonate- independent isoprenoid biosynthesis. Nat Struct Biol. 2001 Jul;8(7):641-8. PMID:11427897 doi:10.1038/89691

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