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
-
mastitis
-
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
-
pnecs
-
biohydrogen
-
hydrogenotrophic
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drug development
-
synthesis
-
analysis
-
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
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Metals Ions
Metals Ions on EC 4.6.1.12 - 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
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Mg2+
Mn2+
Na+
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presence of tetrahedral Zn2+ in one of the metal-binding sites and an octahedral sodium ion in the second metal site in absence of substrate
Zinc
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tightly binds one zinc ion per subunit of the trimer at the active site, which helps to position the substrate for direct attack of the 2-phosphate group on the beta-phosphate
Zn2+
additional information
the tetrahedrally arranged transition metal binding site, potentially occupied by Mn2+, sits at the base of the active site cleft. A phosphate oxygen of 2-C-methyl-D-erythritol-2,4-cyclodiphosphate and the side chains of Asp8, His10, and His42 occupy the metal side chains of Asp8, His10, and His42 occupy the metal side coordination sphere
Mg2+
Mg2+ or Mn2+, positioned between the alpha- and beta-phosphates of the substrate, acts in concert with the Zn2+ to align and polarize the substrate for catalysis
Mn2+
a Mn2+ with octahedral geometry, is positioned between the alpha and beta phosphates acting in concert with the Zn2+ to align and polarize the substrate for catalysis
Mn2+
Mg2+ or Mn2+, positioned between the alpha- and beta-phosphates of the substrate, acts in concert with the Zn2+ to align and polarize the substrate for catalysis
Zn2+
Zn2+-binding site, addition of a Zn2+-binding moiety may prove valuable in assisting the design of potent and selective inhibitors
Zn2+
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presence of tetrahedral Zn2+ in one of the metal-binding sites and an octahedral sodium ion in the second metal site in absence of substrate