Neopikromycin and novapikromycin from the pikromycin biosynthetic pathway of Streptomyces venezuelae

Sang Kil Lee; Je Won Park; Ji Won Kim; Won Seok Jung; Sung Ryeol Park; Cha Yong Choi; Eung Soo Kim; Beom Seok Kim; Jong Seog Ahn; David H. Sherman; Yeo Joon Yoon

doi:10.1021/np060026p

Neopikromycin and novapikromycin from the pikromycin biosynthetic pathway of Streptomyces venezuelae

Sang Kil Lee, Je Won Park, Ji Won Kim, Won Seok Jung, Sung Ryeol Park, Cha Yong Choi, Eung Soo Kim, Beom Seok Kim, Jong Seog Ahn, David H. Sherman, Yeo Joon Yoon

Research output: Contribution to journal › Article › peer-review

44 Citations (Scopus)

Abstract

Two new macrolides from the pikromycin biosynthetic pathway of Streptomyces venezuelae, neopikromycin (9) and novapikromycin (10), were identified and structurally characterized through mass spectrometry and NMR spectroscopy. The established structures showed that 9 and 10 have hydroxyl groups at C-14 (9) and at both C-12 and C-14 (10), on the basis of a comparison with narbomycin (7). The purified PikC cytochrome P450 monooxygenase catalyzes the in vitro hydroxylation of 7 and pikromycin (8) to yield 9 and 10, respectively, thus expanding the substrate- and regio-flexibility of this enzyme.

Original language	English
Pages (from-to)	847-849
Number of pages	3
Journal	Journal of Natural Products
Volume	69
Issue number	5
DOIs	https://doi.org/10.1021/np060026p
Publication status	Published - 2006 May

ASJC Scopus subject areas

Analytical Chemistry
Molecular Medicine
Pharmacology
Pharmaceutical Science
Drug Discovery
Complementary and alternative medicine
Organic Chemistry

Access to Document

10.1021/np060026p

Cite this

@article{ee101ea48f4e496b94c36699787c7a6f,

title = "Neopikromycin and novapikromycin from the pikromycin biosynthetic pathway of Streptomyces venezuelae",

abstract = "Two new macrolides from the pikromycin biosynthetic pathway of Streptomyces venezuelae, neopikromycin (9) and novapikromycin (10), were identified and structurally characterized through mass spectrometry and NMR spectroscopy. The established structures showed that 9 and 10 have hydroxyl groups at C-14 (9) and at both C-12 and C-14 (10), on the basis of a comparison with narbomycin (7). The purified PikC cytochrome P450 monooxygenase catalyzes the in vitro hydroxylation of 7 and pikromycin (8) to yield 9 and 10, respectively, thus expanding the substrate- and regio-flexibility of this enzyme.",

author = "Lee, {Sang Kil} and Park, {Je Won} and Kim, {Ji Won} and Jung, {Won Seok} and Park, {Sung Ryeol} and Choi, {Cha Yong} and Kim, {Eung Soo} and Kim, {Beom Seok} and Ahn, {Jong Seog} and Sherman, {David H.} and Yoon, {Yeo Joon}",

year = "2006",

month = may,

doi = "10.1021/np060026p",

language = "English",

volume = "69",

pages = "847--849",

journal = "Journal of Natural Products",

issn = "0163-3864",

publisher = "American Chemical Society",

number = "5",

}

TY - JOUR

T1 - Neopikromycin and novapikromycin from the pikromycin biosynthetic pathway of Streptomyces venezuelae

AU - Lee, Sang Kil

AU - Park, Je Won

AU - Kim, Ji Won

AU - Jung, Won Seok

AU - Park, Sung Ryeol

AU - Choi, Cha Yong

AU - Kim, Eung Soo

AU - Kim, Beom Seok

AU - Ahn, Jong Seog

AU - Sherman, David H.

AU - Yoon, Yeo Joon

PY - 2006/5

Y1 - 2006/5

N2 - Two new macrolides from the pikromycin biosynthetic pathway of Streptomyces venezuelae, neopikromycin (9) and novapikromycin (10), were identified and structurally characterized through mass spectrometry and NMR spectroscopy. The established structures showed that 9 and 10 have hydroxyl groups at C-14 (9) and at both C-12 and C-14 (10), on the basis of a comparison with narbomycin (7). The purified PikC cytochrome P450 monooxygenase catalyzes the in vitro hydroxylation of 7 and pikromycin (8) to yield 9 and 10, respectively, thus expanding the substrate- and regio-flexibility of this enzyme.

AB - Two new macrolides from the pikromycin biosynthetic pathway of Streptomyces venezuelae, neopikromycin (9) and novapikromycin (10), were identified and structurally characterized through mass spectrometry and NMR spectroscopy. The established structures showed that 9 and 10 have hydroxyl groups at C-14 (9) and at both C-12 and C-14 (10), on the basis of a comparison with narbomycin (7). The purified PikC cytochrome P450 monooxygenase catalyzes the in vitro hydroxylation of 7 and pikromycin (8) to yield 9 and 10, respectively, thus expanding the substrate- and regio-flexibility of this enzyme.

UR - http://www.scopus.com/inward/record.url?scp=33745777367&partnerID=8YFLogxK

U2 - 10.1021/np060026p

DO - 10.1021/np060026p

M3 - Article

C2 - 16724858

AN - SCOPUS:33745777367

SN - 0163-3864

VL - 69

SP - 847

EP - 849

JO - Journal of Natural Products

JF - Journal of Natural Products

IS - 5

ER -

Neopikromycin and novapikromycin from the pikromycin biosynthetic pathway of Streptomyces venezuelae

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this