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Literature summary for 4.6.1.12 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)

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

Protein Variants

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

Metals/Ions

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

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

Synonyms

Synonyms Comment Organism
MECP
-
Escherichia coli