An L-threonine transaldolase is required for L-threo-β-hydroxy-α-amino acid assembly during obafluorin biosynthesis

An L-threonine transaldolase is required for L-threo-β-hydroxy-α-amino acid assembly during obafluorin biosynthesis

Obafluorin is a β-lactone antibiotic produced byPseudomonas fluorescens. Here the authors present the biosynthetic gene cluster and biosynthetic pathway of obafluorin, which is characterized by a central transaldolase step catalysed by a rare L-threonine transaldolase.

Bibliographic Details
Main Authors: Thomas A. Scott, Daniel Heine, Zhiwei Qin, Barrie Wilkinson
Format: Article
Language:English
Published: Nature Publishing Group 2017-06-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms15935
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spelling doaj-7b242d2ca4034e769a1c3a08715872de2021-05-11T07:18:44ZengNature Publishing GroupNature Communications2041-17232017-06-018111110.1038/ncomms15935An L-threonine transaldolase is required for L-threo-β-hydroxy-α-amino acid assembly during obafluorin biosynthesisThomas A. Scott0Daniel Heine1Zhiwei Qin2Barrie Wilkinson3Department of Molecular Microbiology, John Innes CentreDepartment of Molecular Microbiology, John Innes CentreDepartment of Molecular Microbiology, John Innes CentreDepartment of Molecular Microbiology, John Innes CentreObafluorin is a β-lactone antibiotic produced byPseudomonas fluorescens. Here the authors present the biosynthetic gene cluster and biosynthetic pathway of obafluorin, which is characterized by a central transaldolase step catalysed by a rare L-threonine transaldolase.https://doi.org/10.1038/ncomms15935
collection DOAJ
language English
format Article
sources DOAJ
author Thomas A. Scott
Daniel Heine
Zhiwei Qin
Barrie Wilkinson
spellingShingle Thomas A. Scott
Daniel Heine
Zhiwei Qin
Barrie Wilkinson
An L-threonine transaldolase is required for L-threo-β-hydroxy-α-amino acid assembly during obafluorin biosynthesis
Nature Communications
author_facet Thomas A. Scott
Daniel Heine
Zhiwei Qin
Barrie Wilkinson
author_sort Thomas A. Scott
title An L-threonine transaldolase is required for L-threo-β-hydroxy-α-amino acid assembly during obafluorin biosynthesis
title_short An L-threonine transaldolase is required for L-threo-β-hydroxy-α-amino acid assembly during obafluorin biosynthesis
title_full An L-threonine transaldolase is required for L-threo-β-hydroxy-α-amino acid assembly during obafluorin biosynthesis
title_fullStr An L-threonine transaldolase is required for L-threo-β-hydroxy-α-amino acid assembly during obafluorin biosynthesis
title_full_unstemmed An L-threonine transaldolase is required for L-threo-β-hydroxy-α-amino acid assembly during obafluorin biosynthesis
title_sort l-threonine transaldolase is required for l-threo-β-hydroxy-α-amino acid assembly during obafluorin biosynthesis
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-06-01
description Obafluorin is a β-lactone antibiotic produced byPseudomonas fluorescens. Here the authors present the biosynthetic gene cluster and biosynthetic pathway of obafluorin, which is characterized by a central transaldolase step catalysed by a rare L-threonine transaldolase.
url https://doi.org/10.1038/ncomms15935
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