4.6.1.12: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
This is an abbreviated version!
For detailed information about 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, go to the full flat file.
Word Map on EC 4.6.1.12
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4.6.1.12
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electrolysis
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salivary
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mucoepidermoid
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myoepithelial
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milk
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wastewater
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anode
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cathode
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microvascular
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adenoid
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mastitis
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geobacter
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calponin
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stat5
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bioelectrochemical
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caspofungin
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coulomb
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single-chamber
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biocathode
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electroactive
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warthin
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methanogenesis
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posaconazole
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syntrophic
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echinocandins
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voriconazole
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micafungin
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intermediate-grade
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anidulafungin
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bioanode
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pnecs
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biohydrogen
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hydrogenotrophic
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drug development
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synthesis
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analysis
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medicine
- 4.6.1.12
-
electrolysis
-
salivary
-
mucoepidermoid
-
myoepithelial
- milk
-
wastewater
-
anode
-
cathode
-
microvascular
-
adenoid
- mastitis
- geobacter
- calponin
- stat5
-
bioelectrochemical
- caspofungin
-
coulomb
-
single-chamber
-
biocathode
-
electroactive
-
warthin
-
methanogenesis
- posaconazole
-
syntrophic
-
echinocandins
- voriconazole
- micafungin
-
intermediate-grade
- anidulafungin
-
bioanode
-
pnecs
-
biohydrogen
-
hydrogenotrophic
- drug development
- synthesis
- analysis
- medicine
Reaction
Synonyms
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, 2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase, 2-methylerythritol 2,4-cyclodiphosphate synthase, 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase, 2C-methyl-D-erythrol-2,4-cyclodiphosphate synthase, cMEPP synthase, IspDF, IspE, IspF, MCS, MDS, ME-CPP synthase, MEC synthase, MECDP synthase, MECDP-synthase, MECP, MECPS, MECS, YGBB, YgbB protein
ECTree
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Crystallization
Crystallization on EC 4.6.1.12 - 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
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in complex with cytidine 5-monophosphate, at 2.3 A resolution. In contrast to bacterial enzymes, the cavity of Arabidopsis thaliana structure is unsuited for binding a diphosphate moiety
structures of native IspF and in complex with CMP, to 1.99 A resolution
hanging drop vapor diffusion method, crystal structure of IspDF, a bifunctional methylerythritol 4-phosphate cytidyltransferase methylerythritol 2,4-cyclodidiphosphate synthase
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computational model of binding of inhibitor N-[4-[(6-aminopyridin-3-yl)amino]-3-methylbenzyl]-4-(trifluoromethyl)benzamide in the active site
hanging-drop vapour diffusion method, X-ray crystal structures refined to 2.8 A resolution. The first structure contains a bound Mn2+ cation and the second structure contains CMP, 2-C-methyl-D-erythritol-2,4-cyclodiphosphate, and Mn2+
IspF-CDP complex, to 1.8 A resolution. IspF in complex with compound 6b, to 3.1 A resolution, belongs to space group I213 with unit cell parameter a = 144 A. IspF in complex with compound 7, to 2.7 A resolution, belongs to space group I213 with unit cell parameter a = 144.5 A. IspF in complex with cytosine arabinoside monophosphate, to 2.1 A resolution, belongs to space group P21 with unit cell parameters a = 88.8 A, b = 54.2 A, c = 118.4 A, beta = 95°. IspF in complex with 5-fluorocytidine, to 2.5 A resolution, belongs to space group C2 with unit cell parameters a = 104.68 A, b = 54.83 A, c = 88.51 A, beta = 99.66°. IspF in complex with cidofovir, to 2.8 A resolution, belongs to space group I213 with unit cell parameter a = 145.68 A
vapor-diffusion hanging drop method, crystal structure of the zinc enzyme in complex with cytidine 5'-diphosphate and Mn2+ is determined to 1.8 A resolution
high-resolution structure, 16 A, of the enzyme in absence of substrate in the active site. Optimized crystals are obtained at a protein concentration of 35 mg/ml in a solution containing 4 M sodium formate and 5% glycerol. The crystals grow to avarage dimensions of 0.4 * 0.3 * 0.3 mM within a week
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crystals grow in space group P4(1)2(1)2 from polyethylene glycol using the hanging-drop method