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Literature summary extracted from

  • Sgraja, T.; Kemp, L.E.; Ramsden, N.; Hunter, W.N.
    A double mutation of Escherichia coli 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to prevent binding of, an isoprenoid diphosphate (2005), Acta Crystallogr. Sect. F, F61, 625-629.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.6.1.12 3.1 A resolution crystal structure of the Met142/Leu144 mutant Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.12 Arg142Met, Glu144Leu dual mutation with little influence on both the overall structure and the detail in the active site Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.6.1.12 Mn2+
-
 Escherichia coli
4.6.1.12 Zn2+
-
 Escherichia coli

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
-
 Escherichia coli 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.6.1.12 MECP
-
 Escherichia coli