Linear Peptides Are the Major Products of a Biosynthetic Pathway That Encodes for Cyclic Depsipeptides

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

Standard

Linear Peptides Are the Major Products of a Biosynthetic Pathway That Encodes for Cyclic Depsipeptides. / Wyche, Thomas P.; Ruzzini, Antonio C.; Beemelmanns, Christine; Kim, Ki Hyun; Klassen, Jonathan L.; Cao, Shugeng; Thomas-Poulsen, Michael; Bugni, Tim S.; Currie, Cameron R.; Clardy, Jon.

In: Organic Letters, Vol. 19, No. 7, 2017, p. 1772-1775.

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

Harvard

Wyche, TP, Ruzzini, AC, Beemelmanns, C, Kim, KH, Klassen, JL, Cao, S, Thomas-Poulsen, M, Bugni, TS, Currie, CR & Clardy, J 2017, 'Linear Peptides Are the Major Products of a Biosynthetic Pathway That Encodes for Cyclic Depsipeptides', Organic Letters, vol. 19, no. 7, pp. 1772-1775. https://doi.org/10.1021/acs.orglett.7b00545

APA

Wyche, T. P., Ruzzini, A. C., Beemelmanns, C., Kim, K. H., Klassen, J. L., Cao, S., Thomas-Poulsen, M., Bugni, T. S., Currie, C. R., & Clardy, J. (2017). Linear Peptides Are the Major Products of a Biosynthetic Pathway That Encodes for Cyclic Depsipeptides. Organic Letters, 19(7), 1772-1775. https://doi.org/10.1021/acs.orglett.7b00545

Vancouver

Wyche TP, Ruzzini AC, Beemelmanns C, Kim KH, Klassen JL, Cao S et al. Linear Peptides Are the Major Products of a Biosynthetic Pathway That Encodes for Cyclic Depsipeptides. Organic Letters. 2017;19(7):1772-1775. https://doi.org/10.1021/acs.orglett.7b00545

Author

Wyche, Thomas P. ; Ruzzini, Antonio C. ; Beemelmanns, Christine ; Kim, Ki Hyun ; Klassen, Jonathan L. ; Cao, Shugeng ; Thomas-Poulsen, Michael ; Bugni, Tim S. ; Currie, Cameron R. ; Clardy, Jon. / Linear Peptides Are the Major Products of a Biosynthetic Pathway That Encodes for Cyclic Depsipeptides. In: Organic Letters. 2017 ; Vol. 19, No. 7. pp. 1772-1775.

Bibtex

@article{74a24d5d17524973b8a05d1d7c82b740,
title = "Linear Peptides Are the Major Products of a Biosynthetic Pathway That Encodes for Cyclic Depsipeptides",
abstract = "Three new dentigerumycin analogues are produced by Streptomyces sp. M41, a bacterium isolated from a South African termite, Macrotermes natalensis. The structures of the complex nonribosomal peptide synthetase-polyketide synthase (NRPS/PKS) hybrid compounds were determined by 1D- and 2D-NMR spectroscopy, high-resolution mass spectrometry, and circular dichroism (CD) spectroscopy. Both cyclic and linear peptides are reported, and the genetic organization of the NRPS modules within the biosynthetic gene cluster accounts for the observed structural diversity.",
author = "Wyche, {Thomas P.} and Ruzzini, {Antonio C.} and Christine Beemelmanns and Kim, {Ki Hyun} and Klassen, {Jonathan L.} and Shugeng Cao and Michael Thomas-Poulsen and Bugni, {Tim S.} and Currie, {Cameron R.} and Jon Clardy",
year = "2017",
doi = "10.1021/acs.orglett.7b00545",
language = "English",
volume = "19",
pages = "1772--1775",
journal = "Organic Letters",
issn = "1523-7060",
publisher = "American Chemical Society",
number = "7",

}

RIS

TY - JOUR

T1 - Linear Peptides Are the Major Products of a Biosynthetic Pathway That Encodes for Cyclic Depsipeptides

AU - Wyche, Thomas P.

AU - Ruzzini, Antonio C.

AU - Beemelmanns, Christine

AU - Kim, Ki Hyun

AU - Klassen, Jonathan L.

AU - Cao, Shugeng

AU - Thomas-Poulsen, Michael

AU - Bugni, Tim S.

AU - Currie, Cameron R.

AU - Clardy, Jon

PY - 2017

Y1 - 2017

N2 - Three new dentigerumycin analogues are produced by Streptomyces sp. M41, a bacterium isolated from a South African termite, Macrotermes natalensis. The structures of the complex nonribosomal peptide synthetase-polyketide synthase (NRPS/PKS) hybrid compounds were determined by 1D- and 2D-NMR spectroscopy, high-resolution mass spectrometry, and circular dichroism (CD) spectroscopy. Both cyclic and linear peptides are reported, and the genetic organization of the NRPS modules within the biosynthetic gene cluster accounts for the observed structural diversity.

AB - Three new dentigerumycin analogues are produced by Streptomyces sp. M41, a bacterium isolated from a South African termite, Macrotermes natalensis. The structures of the complex nonribosomal peptide synthetase-polyketide synthase (NRPS/PKS) hybrid compounds were determined by 1D- and 2D-NMR spectroscopy, high-resolution mass spectrometry, and circular dichroism (CD) spectroscopy. Both cyclic and linear peptides are reported, and the genetic organization of the NRPS modules within the biosynthetic gene cluster accounts for the observed structural diversity.

U2 - 10.1021/acs.orglett.7b00545

DO - 10.1021/acs.orglett.7b00545

M3 - Letter

C2 - 28326787

AN - SCOPUS:85017179138

VL - 19

SP - 1772

EP - 1775

JO - Organic Letters

JF - Organic Letters

SN - 1523-7060

IS - 7

ER -

ID: 199558504