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Literature summary for 2.7.7.60 extracted from

  • Richard, S.B.; Bowman, M.E.; Kwiatkowski, W.; Kang, L.; Chow, C.; Lillo, A.M.; Cane, D.E.; Noel, J.P.
    Structure of 4-diphosphocytidyl-2-C-methylerythritol synthetase involved in mevalonate-independent isoprenoid biosynthesis (2001), Nature Struct. Biol., 8, 641-648.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
vapor diffusion method at 4°C in hanging drops, crystals belong to space group C2 Escherichia coli

Protein Variants

Protein Variants Comment Organism
K213S effective turnover rate is ca. 0.4% of the rate of wild type, retains capacity to form product with significantly reduced efficiency Escherichia coli
K27A amino acid plays an essential role in catalysis because the effective turnover rate is ca. 0.025% of the rate of wild type enzyme Escherichia coli
K27S amino acid plays an essential role in catalysis because the effective turnover rate is ca. 0.025% of the rate of wild type enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ essential for activity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CTP + 2-C-methyl-D-erythritol-4-phosphate Mycobacterium tuberculosis
-
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate Plasmodium falciparum
-
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate Escherichia coli third step of biosynthesis diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate Escherichia coli part of mevalonate-indpendent pathway for isoprenoid biosynthesis diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Mycobacterium tuberculosis
-
-
-
Plasmodium falciparum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-nitrilotriacetic acid column Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol cytidyltransferase family. Active substrate site consists of a glycine-rich loop spanning Pro13-Arg20. Three-dimensional structure of enzyme is figured out Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CTP + 2-C-methyl-D-erythritol 4-phosphate
-
Escherichia coli diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
-
Mycobacterium tuberculosis diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
-
Plasmodium falciparum diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate third step of biosynthesis Escherichia coli diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate part of mevalonate-indpendent pathway for isoprenoid biosynthesis Escherichia coli diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
?

Subunits

Subunits Comment Organism
dimer homodimer Escherichia coli
dimer each subunit contains a globular core domain with an alpha/beta sturcture and and one smaller subdomain Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Escherichia coli