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Literature summary 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

EC Number Activating Compound Comment Organism Structure
4.2.1.51 L-methionine activation Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.51 35000
-
 2 * 35000, low activity in absence of activators, high activity in presence of activators Bacillus subtilis
4.2.1.51 35000
-
 8 * 35000, presence of activating molecules Bacillus subtilis
4.2.1.51 210000
-
 presence of activating molecules, gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.51 Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.2.1.51
-
 4 diluted enzyme stable for several hours Bacillus subtilis
4.2.1.51 32
-
 60 min, dissociation of 210000 MW enzyme to inactive 35000 Da units Bacillus subtilis