کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1391183 983216 2013 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Biosynthetic Conclusions from the Functional Dissection of Oxygenases for Biosynthesis of Actinorhodin and Related Streptomyces Antibiotics
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آلی
پیش نمایش صفحه اول مقاله
Biosynthetic Conclusions from the Functional Dissection of Oxygenases for Biosynthesis of Actinorhodin and Related Streptomyces Antibiotics
چکیده انگلیسی

SummaryActinorhodin (ACT) produced by Streptomyces coelicolor A3(2) belongs to the benzoisochromanequinone (BIQ) class of antibiotics. ActVA-ORF5, a flavin-dependent monooxygenase (FMO) essential for ACT biosynthesis, forms a two-component enzyme system in combination with a flavin:NADH oxidoreductase, ActVB. The genes for homologous two-component FMOs are found in the biosynthetic gene clusters for two other BIQs, granaticin (GRA) and medermycin (MED), and a closely related antibiotic, alnumycin (ALN). Our functional analysis of these FMOs (ActVA-ORF5, Gra-ORF21, Med-ORF7, and AlnT) in S. coelicolor unambiguously demonstrated that ActVA-ORF5 and Gra-ORF21 are bifunctional and capable of both p-quinone formation at C-6 in the central ring and C-8 hydroxylation in the lateral ring, whereas Med-ORF7 catalyzes only p-quinone formation. No p-quinone formation on a BIQ substrate was observed for AlnT, which is involved in lateral p-quinone formation in ALN.

Graphical AbstractFigure optionsDownload high-quality image (332 K)Download as PowerPoint slideHighlights
► ActVA-ORF5 is a flavin-dependent monooxygenase required for actinorhodin biosynthesis
► ActVA-ORF5 and its three close homologs were functionally dissected
► ActVA-ORF5 and Gra-21 are bifunctional at C-6/C-8, while Med-7 acts only for C-6
► AlnT exhibits different regiospecificity for oxidation of tricyclic substrates

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: - Volume 20, Issue 4, 18 April 2013, Pages 510–520
نویسندگان
, , , , , , , ,