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Literature summary extracted from

  • Steinbacher, S.; Kaiser, J.; Wungsintaweekul, J.; Hecht, S.; Eisenreich, W.; Gerhardt, S.; Bacher, A.; Rohdich, F.
    Structure of 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids (2002), J. Mol. Biol., 316, 79-88.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.6.1.12
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.6.1.12 Mg2+ dependent on Escherichia coli
4.6.1.12 Zinc 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 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.6.1.12 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol Escherichia coli involved in mevalonate-independent biosynthesis of isoprenoids 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.12 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.12 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol involved in mevalonate-independent biosynthesis of isoprenoids Escherichia coli 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP
-
 ?

Subunits

EC Number Subunits Comment Organism
4.6.1.12 trimer
-
 Escherichia coli