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Literature summary extracted from

  • Richter, M.; Traitcheva, N.; Knuepfer, U.; Hertweck, C.
    Sequential asymmetric polyketide heterocyclization catalyzed by a single cytochrome p450 monooxygenase (AurH) (2008), Angew. Chem. Int. Ed. Engl., 47, 8872-8875 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.37 expression in Escherichia coli Streptomyces thioluteus

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.37 Streptomyces thioluteus Q70KH6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.37 (7R)-7-hydroxyluteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Streptomyces thioluteus aureothin + 2 H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.14.15.37 luteothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+
-
 Streptomyces thioluteus aureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.14.15.37 luteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Streptomyces thioluteus (7R)-7-hydroxyluteothin + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.14.15.37 additional information the formation of the heterocycle is catalyzed by a single enzyme both in vivo and in vitro. The reaction is a sequential hydroxylation-heterocyclization sequence. The methylene position adjacent to the pyrone ring (C7) is attacked first, which defines the absolute configuration of the resulting heterocycle. The second allylic position (C9a) is then oxygenated by the adjacent hydroxymethyl group Streptomyces thioluteus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.37 AurH
-
 Streptomyces thioluteus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.37 cytochrome P450
-
 Streptomyces thioluteus