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Literature summary for 4.1.1.100 extracted from

  • Mahlstedt, S.A.; Walsh, C.T.
    Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis (2010), Biochemistry, 49, 912-923.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.100

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
 prephenate pH 8, 22°C Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prephenate Bacillus subtilis the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
 ?
prephenate Bacillus subtilis 168 the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P39638
-
-
Bacillus subtilis 168 P39638
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin Bacillus subtilis 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
 ?
prephenate decarboxylation and protonation at C6', with a shift of the participating double bond from the C5'-6' position to the C4-9 position Bacillus subtilis 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2 the product can undergo a nonenzymatic isomerization to produce 3-(4-hydroxycyclohex-2-enylidene)-2-oxopropanoate ?
prephenate the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin Bacillus subtilis 168 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
 ?
prephenate decarboxylation and protonation at C6', with a shift of the participating double bond from the C5'-6' position to the C4-9 position Bacillus subtilis 168 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2 the product can undergo a nonenzymatic isomerization to produce 3-(4-hydroxycyclohex-2-enylidene)-2-oxopropanoate ?

Synonyms

Synonyms Comment Organism
bacA
-
 Bacillus subtilis
non-aromatizing prephenate decarboxylase
-
 Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2
-
 prephenate pH 8, 22°C Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bacillus subtilis

General Information

General Information Comment Organism
physiological function the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin Bacillus subtilis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
45.2
-
 prephenate pH 8, 22°C Bacillus subtilis