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Literature summary for 4.6.1.12 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)

Crystallization (Comment) Organism
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Escherichia coli
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Subunits Comment Organism
trimer
-
Escherichia coli