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Literature summary for 4.2.1.51 extracted from

  • Riepl, R.G.; Glover, G.I.
    Regulation and state of aggregation of Bacillus subtilis prephenate dehydratase in the presence of allosteric effectors (1979), J. Biol. Chem., 254, 10321-10328.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
L-methionine activation Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
2 * 35000, low activity in absence of activators, high activity in presence of activators Bacillus subtilis
35000
-
8 * 35000, presence of activating molecules Bacillus subtilis
210000
-
presence of activating molecules, gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prephenate Bacillus subtilis
-
?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate
-
Bacillus subtilis phenylpyruvate + H2O + CO2
-
?
prephenate
-
Bacillus subtilis ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 35000, low activity in absence of activators, high activity in presence of activators Bacillus subtilis
octamer 8 * 35000, presence of activating molecules Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
4 diluted enzyme stable for several hours Bacillus subtilis
32
-
60 min, dissociation of 210000 MW enzyme to inactive 35000 Da units Bacillus subtilis