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Literature summary for 4.1.1.100 extracted from

  • Mahlstedt, S.; Fielding, E.N.; Moore, B.S.; Walsh, C.T.
    Prephenate decarboxylases: a new prephenate-utilizing enzyme family that performs nonaromatizing decarboxylation en route to diverse secondary metabolites (2010), Biochemistry, 49, 9021-9023.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli with an N-terminal His6 tag Planktothrix agardhii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.17
-
prephenate pH and temperature not specified in the publication Planktothrix agardhii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prephenate Planktothrix agardhii the enzyme is involved in the biosynthesis of the nonribosomal glycopeptides aeruginoside 126A and B. These natural products contain the unusual amino acid residue 2-carboxy-6-hydroxy-octahydroindole 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2 the product is non-enzymatically isomerized to the thermodynamically favored conjugated exocyclic diene 3-((1R,4R)-4-hydroxycyclohexa-2-enylidene)-2-oxopropanoate ?
prephenate Salinispora tropica the enzyme is involved in the biosynthetic pathway to the proteasome inhibitor salinosporamide A. SalX is relevant to the production of the nonproteinogenic amino acid building block cyclohexenylalanine 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Planktothrix agardhii
-
-
-
Salinispora tropica
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Planktothrix agardhii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prephenate
-
Salinispora tropica 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
?
prephenate
-
Planktothrix agardhii 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
?
prephenate the enzyme is involved in the biosynthesis of the nonribosomal glycopeptides aeruginoside 126A and B. These natural products contain the unusual amino acid residue 2-carboxy-6-hydroxy-octahydroindole Planktothrix agardhii 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2 the product is non-enzymatically isomerized to the thermodynamically favored conjugated exocyclic diene 3-((1R,4R)-4-hydroxycyclohexa-2-enylidene)-2-oxopropanoate ?
prephenate the enzyme is involved in the biosynthetic pathway to the proteasome inhibitor salinosporamide A. SalX is relevant to the production of the nonproteinogenic amino acid building block cyclohexenylalanine Salinispora tropica 3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
?

Synonyms

Synonyms Comment Organism
aerD
-
Planktothrix agardhii
SalX
-
Salinispora tropica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1
-
prephenate pH and temperature not specified in the publication Planktothrix agardhii

General Information

General Information Comment Organism
physiological function the enzyme is involved in the biosynthesis of the nonribosomal glycopeptides aeruginoside 126A and B. These natural products contain the unusual amino acid residue 2-carboxy-6-hydroxy-octahydroindole Planktothrix agardhii
physiological function the enzyme is involved in the biosynthetic pathway to the proteasome inhibitor salinosporamide A. SalX is relevant to the production of the nonproteinogenic amino acid building block cyclohexenylalanine Salinispora tropica

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
12.2
-
prephenate pH and temperature not specified in the publication Salinispora tropica
24
-
prephenate pH and temperature not specified in the publication Planktothrix agardhii