Two Cytochrome P450 Enzymes from Streptomyces sp. NRRL S‑1868 Catalyze Distinct Dimerization of Tryptophan-Containing Cyclodipeptides

Heterologous expression in Streptomyces coelicolor and in vitro enzyme characterization proved that two P450 enzymes, AspB and NasB, from Streptomyces sp. NRRL S-1868 catalyze two new dimerization patterns of tryptophan-containing cyclodipeptides. Structure elucidation of the metabolites revealed an...

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Veröffentlicht in:Organic letters 2019-09, Vol.21 (17), p.7094-7098
Hauptverfasser: Yu, Huili, Li, Shu-Ming
Format: Artikel
Sprache:eng
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Zusammenfassung:Heterologous expression in Streptomyces coelicolor and in vitro enzyme characterization proved that two P450 enzymes, AspB and NasB, from Streptomyces sp. NRRL S-1868 catalyze two new dimerization patterns of tryptophan-containing cyclodipeptides. Structure elucidation of the metabolites revealed an N1–C7′ dimer of two cWP molecules as the predominant product of AspB and C3–C7′ connected cWP with cWA as that of NasB.
ISSN:1523-7060
1523-7052
DOI:10.1021/acs.orglett.9b02666