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Literature summary for 5.4.99.5 extracted from

  • Lorence, J.H.; Nester, E.W.
    Multiple molecular forms of chorismate mutase in Bacillus subtilis (1967), Biochemistry, 6, 1541-1553.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
chorismate strain WB672, inhibition above 2 mM Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1
-
chorismate strain WB672 Bacillus subtilis
2.6
-
chorismate strain 168 Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
75000
-
enzyme form CM1, gel filtration Bacillus subtilis
140000
-
chorismate mutase/prephenate dehydratase, enzyme form CM2, gel filtration Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
strain 23 and its derivatives have 3 distinct enzyme species: CM1, CM2, and CM3. Strain 168 has only the CM3 form. Enzyme forms CM1 and CM2 may represent different aggregation states involving at least one common subunit
-
Bacillus subtilis 23
-
strain 23 and its derivatives have 3 distinct enzyme species: CM1, CM2, and CM3. Strain 168 has only the CM3 form. Enzyme forms CM1 and CM2 may represent different aggregation states involving at least one common subunit
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Chorismate
-
Bacillus subtilis Prephenate
-
?
Chorismate
-
Bacillus subtilis 23 Prephenate
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
14 min, strain 168, stable Bacillus subtilis
60
-
10 min, strain 672, 90% loss of activity Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.6
-
-
Bacillus subtilis
8.9
-
high activity strain WB672 Bacillus subtilis