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

11 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.

Funding

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.

Funders	Funder number
Deutsche Forschungs-gemeinschaft	6-1
National Institutes of Health (NIH)
National Childhood Cancer Registry – National Cancer Institute	R01CA102102

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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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

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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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JF - Journal of Biotechnology

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

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

Access to Document

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