Surprising production of a new urdamycin derivative by S. fradiae ΔurdQ/R

M. Fedoryshyn; M. Nur-e-Alam; L. Zhu; A. Luzhetskyy; J. Rohr; A. Bechthold

doi:10.1016/j.jbiotec.2007.02.018

Surprising production of a new urdamycin derivative by S. fradiae ΔurdQ/R

M. Fedoryshyn, M. Nur-e-Alam, L. Zhu, A. Luzhetskyy, J. Rohr, A. Bechthold

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

10 Scopus citations

Abstract

A strain (S. fradiae ΔurdQ/R) with mutations in urdQ and urdR encoding a dTDP-hexose-3,4-dehydratase and a dTDP-hexose-4-ketoreductase, respectively, produces a new urdamycin analogue (urdamycin X) with changes in the polyketide structure. The structure of urdamycin X has been elucidated by NMR spectroscopy. Urdamycin X was not detectable, even in small amounts, in either S. fradiae ΔurdQ, in S. fradiae ΔurdR or in S. fradiae A0, a mutant lacking all glycosyltransferase genes. Complementation of S. fradiae ΔurdQ/R restored urdamycin A production indicating that the mutations did not cause any polar effect.

Original language	English
Pages (from-to)	32-38
Number of pages	7
Journal	Journal of Biotechnology
Volume	130
Issue number	1
DOIs	https://doi.org/10.1016/j.jbiotec.2007.02.018
State	Published - May 31 2007

Bibliographical note

Funding Information:
This work was supported by the Deutsche Forschungs-gemeinschaft (DFG) grant 6-1 to A.B. and by NIH grant CA 102102 to J.R. We thank Prof. Dr. J. Salas for providing plasmids pLR234Δ7 and pUC18U.

Keywords

Deoxysugar biosynthetic enzymes
Secondary metabolism
Streptomyces fradiae
Urdamycins

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1016/j.jbiotec.2007.02.018

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title = "Surprising production of a new urdamycin derivative by S. fradiae ΔurdQ/R",

abstract = "A strain (S. fradiae ΔurdQ/R) with mutations in urdQ and urdR encoding a dTDP-hexose-3,4-dehydratase and a dTDP-hexose-4-ketoreductase, respectively, produces a new urdamycin analogue (urdamycin X) with changes in the polyketide structure. The structure of urdamycin X has been elucidated by NMR spectroscopy. Urdamycin X was not detectable, even in small amounts, in either S. fradiae ΔurdQ, in S. fradiae ΔurdR or in S. fradiae A0, a mutant lacking all glycosyltransferase genes. Complementation of S. fradiae ΔurdQ/R restored urdamycin A production indicating that the mutations did not cause any polar effect.",

keywords = "Deoxysugar biosynthetic enzymes, Secondary metabolism, Streptomyces fradiae, Urdamycins",

author = "M. Fedoryshyn and M. Nur-e-Alam and L. Zhu and A. Luzhetskyy and J. Rohr and A. Bechthold",

note = "Funding Information: This work was supported by the Deutsche Forschungs-gemeinschaft (DFG) grant 6-1 to A.B. and by NIH grant CA 102102 to J.R. We thank Prof. Dr. J. Salas for providing plasmids pLR234Δ7 and pUC18U.",

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doi = "10.1016/j.jbiotec.2007.02.018",

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AU - Nur-e-Alam, M.

AU - Zhu, L.

AU - Luzhetskyy, A.

AU - Rohr, J.

AU - Bechthold, A.

N1 - Funding Information: This work was supported by the Deutsche Forschungs-gemeinschaft (DFG) grant 6-1 to A.B. and by NIH grant CA 102102 to J.R. We thank Prof. Dr. J. Salas for providing plasmids pLR234Δ7 and pUC18U.

PY - 2007/5/31

Y1 - 2007/5/31

N2 - A strain (S. fradiae ΔurdQ/R) with mutations in urdQ and urdR encoding a dTDP-hexose-3,4-dehydratase and a dTDP-hexose-4-ketoreductase, respectively, produces a new urdamycin analogue (urdamycin X) with changes in the polyketide structure. The structure of urdamycin X has been elucidated by NMR spectroscopy. Urdamycin X was not detectable, even in small amounts, in either S. fradiae ΔurdQ, in S. fradiae ΔurdR or in S. fradiae A0, a mutant lacking all glycosyltransferase genes. Complementation of S. fradiae ΔurdQ/R restored urdamycin A production indicating that the mutations did not cause any polar effect.

AB - A strain (S. fradiae ΔurdQ/R) with mutations in urdQ and urdR encoding a dTDP-hexose-3,4-dehydratase and a dTDP-hexose-4-ketoreductase, respectively, produces a new urdamycin analogue (urdamycin X) with changes in the polyketide structure. The structure of urdamycin X has been elucidated by NMR spectroscopy. Urdamycin X was not detectable, even in small amounts, in either S. fradiae ΔurdQ, in S. fradiae ΔurdR or in S. fradiae A0, a mutant lacking all glycosyltransferase genes. Complementation of S. fradiae ΔurdQ/R restored urdamycin A production indicating that the mutations did not cause any polar effect.

KW - Deoxysugar biosynthetic enzymes

KW - Secondary metabolism

KW - Streptomyces fradiae

KW - Urdamycins

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Surprising production of a new urdamycin derivative by S. fradiae ΔurdQ/R

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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