Identification and characterization of <Emphasis Type="Italic">gerPI</Emphasis> and <Emphasis Type="Italic">gerPII</Emphasis> involved in epoxidation and hydroxylation of dihydrochalcolactone in <Emphasis Type="Italic">Streptomyces</Emphasis> species KCTC 0041BP |
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Authors: | Sailesh Malla Ta Thi Thu Thuy Tae Jin Oh Jae Kyung Sohng |
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Institution: | (1) Institute of Biomolecule Reconstruction (iBR), Department of Pharmaceutical Engineering, SunMoon University, # 100 Kalsan-ri, Asansi, Chungnam, 336-708, Korea; |
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Abstract: | The macrolide antibiotics are biosynthesized by initial assembly of a macrolactone ring, followed by a series of post-polyketide
(PKS) modifications. In general, the additional hydroxyl or epoxy groups are installed by cytochrome P450 enzymes, improving
the bioactivity profile through structural diversification of natural products. The biosynthetic gene cluster for the 16-membered
macrolide antibiotic dihydrochalcomycin (DHC) has been cloned from Streptomyces sp. KCTC 0041BP. Three cytochrome P450 genes are found in the DHC biosynthetic gene (ger) cluster. Two P450 enzymes were characterized from this cluster. Disruption of gerPI accumulated predominantly 12,13-de-epoxydihydrochalcomycin while disruption of gerPII accumulated 8-dehydroxy-12,13-de-epoxydihydrochalcomycin; DHC production was abolished in both cases. The results suggest
that GerPII P450 catalyzes hydroxylation at the C8 position followed by an epoxidation reaction catalyzed by GerPI P450 at the C12–C13 position. |
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