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Literature summary for 4.2.1.51 extracted from

  • Fischer, R.; Jensen, R.
    Prephenate dehydratase (monofunctional) (1987), Methods Enzymol., 142, 507-512.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
L-leucine activation Bacillus subtilis
L-methionine activation Bacillus subtilis

General Stability

General Stability Organism
octameric form, whose aggregation is caused by activator molecules is stable, while the dimeric form can be stabilized by glycerol Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
L-phenylalanine
-
Bacillus subtilis
L-tryptophan
-
Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
1 * 35000, inactive enzyme in absence of activating molecules Bacillus subtilis
35000
-
2 * 35000, slightly active Bacillus subtilis
35000
-
8 * 35000, presence of activating molecules Bacillus subtilis
55000
-
absence of activating molecules, gel filtration 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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
17.5
-
-
Bacillus subtilis

Storage Stability

Storage Stability Organism
4°C, 20% glycerol or presence of L-Met, L-Leu, prephenate, stable for several months 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, slightly active Bacillus subtilis
monomer 1 * 35000, inactive enzyme in absence of activating molecules Bacillus subtilis
octamer 8 * 35000, presence of activating molecules Bacillus subtilis