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.
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 |
Similar Items
-
The biosynthesis of obafluorin and related metabolites
by: Knaggs, Andrew Richard
Published: (1990) -
Biosynthesis and mode of action of the β-lactone antibiotic obafluorin
by: Scott, Thomas
Published: (2017) -
Transaldolase of Methanocaldococcus jannaschii
by: Tim Soderberg, et al.
Published: (2004-01-01) -
threo-Diethyl 2-ethyl-2-hydroxy-3-(4-methylbenzenesulfonamido)succinate
by: Sofiane Mekki, et al.
Published: (2011-08-01) -
I. The Synthesis of D- and L-Threo- and D- and L-Erythro-α-Amino-β-hydroxy-n-caproic Acids. II. Experiments on the Preparation of α-Aminoalkanesulfonamides. III. The Influence of Nerve Impulse Sequence on the Contractions of Different Crustacean Muscles
by: Adams, Robert Train
Published: (1950)