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Literature summary for 2.6.1.28 extracted from

  • Balibar, C.J.; Howard-Jones, A.R.; Walsh, C.T.
    Terrequinone A biosynthesis through L-tryptophan oxidation, dimerization and bisprenylation (2007), Nat. Chem. Biol., 3, 584-592.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of complete gene cluster TdiA-TdiE in Escherichia coli, in order to establish the biosynthetic pathway to terrequinone A Aspergillus nidulans

Protein Variants

Protein Variants Comment Organism
additional information expression of complete gene cluster TdiA-TdiE in Escherichia coli, in order to establish the biosynthetic pathway to terrequinone A Aspergillus nidulans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.198
-
L-tryptophan pH 7.8 Aspergillus nidulans

Organism

Organism UniProt Comment Textmining
Aspergillus nidulans A7XRY8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + phenylpyruvate pyruvate, 2-oxoglutarate, and 2-oxo-(4-methylthio)butyrateare no co-substrates Aspergillus nidulans 3-indole-2-oxopropanoate + L-phenylalanine for biosynthesis of terrequinone A, 3-indole-2-oxopropanoate is used for an unusual nonoxidative coupling by the tridomain nonribosomal peptide synthetase TdiA ?

Synonyms

Synonyms Comment Organism
TdiD
-
Aspergillus nidulans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0032
-
L-tryptophan pH 7.8 Aspergillus nidulans

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Aspergillus nidulans