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Literature summary for 5.4.99.5 extracted from

  • Mandal, A.; Hilvert, D.
    Charge optimization increases the potency and selectivity of a chorismate mutase inhibitor (2003), J. Am. Chem. Soc., 125, 5598-5599.
    View publication on PubMed
Search for more literature for 5.4.99.5

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
DELTA117-127 lower turnover and lower KM than wild-type enzyme Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
 Bacillus subtilis
(1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate
-
 Escherichia coli
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
 Bacillus subtilis
(1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
 Escherichia coli
(1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
 Bacillus subtilis
(1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.074
-
 chorismate wild-type Bacillus subtilis
0.39
-
 chorismate chorismate mutase domain of P-protein Escherichia coli
9.6
-
 chorismate DELTA 117-127 Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Chorismate Bacillus subtilis shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine Prephenate
-
 ?
Chorismate Escherichia coli shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine Prephenate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Chorismate
-
 Bacillus subtilis Prephenate
-
 ?
Chorismate
-
 Escherichia coli Prephenate
-
 ?
Chorismate shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine Bacillus subtilis Prephenate
-
 ?
Chorismate shikimate pathway in bacteria, fungi and higher plants that leads to tyrosine and phenylalanine Escherichia coli Prephenate
-
 ?

Synonyms

Synonyms Comment Organism
BsCM
-
 Bacillus subtilis
chorismate mutase
-
 Bacillus subtilis
chorismate mutase
-
 Escherichia coli
EcCM
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2 8 chorismate mutant DELTA117-127 Bacillus subtilis
41
-
 chorismate wild-type Bacillus subtilis
64
-
 chorismate chorismate mutase domain of P-protein Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00032
-
 (1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid 30°C, pH 7.5, wild-type Bacillus subtilis
0.001
-
 (1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate 30°C, pH 7.5, wild-type Bacillus subtilis
0.0023
-
 (1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate 30°C, pH 7.5, chorismate mutase domain of P-protein Escherichia coli
0.0029
-
 (1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid 30°C, pH 7.5, mutant DELTA117-127 Bacillus subtilis
0.0076
-
 (1S,3R,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid 30°C, pH 7.5, chorismate mutase domain of P-protein Escherichia coli
0.051
-
 (1R,3R,5S)-3-carboxy-1-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-5-carboxylate 30°C, pH 7.5, mutant DELTA117-127 Bacillus subtilis
0.23
-
 (1S,3S,5R)-1-hydroxy-5-nitro-2-oxabicyclo[3.3.1]non-6-ene-3-carboxylic acid 30°C, pH 7.5, wild-type Bacillus subtilis