|
type |
Journal Article |
authors |
Yun X, Zhang Q, Lv M, Deng H, Deng Z, Yu Y. |
title |
In vitro reconstitution of the biosynthetic pathway of 3-hydroxypicolinic acid |
journal |
Org Biomol Chem |
Activity |
l-lysine.2-aminotransferase |
Family |
l-lysine.2-aminotransferase.a |
sel |
selected |
ui |
30565646 |
year |
(2019) |
volume |
17 |
number |
3 |
pages |
454-460 |
| |
keywords |
doi: 10.1039/c8ob02972e |
abstract |
3-Hydroxypicolinic acid (3-HPA) is an important pyridine building block of bacterial secondary metabolites. Although the main biosynthetic pathways of these metabolites have been identified and well characterized, the enzymatic mechanism underlying the biosynthesis of 3-HPA has yet to be elucidated. In this work, we successfully reconstituted the complete biosynthetic pathway of 3-HPA in vitro. We showed that an l-lysine 2-aminotransferase, a two-component monooxygenase, and a FAD-dependent dehydrogenase are required to convert l-lysine to 3-HPA. We further demonstrated that 3-HPA does not derive from the direct hydroxylation of the picolinic acid at C-3, but from a successive process of C-3 hydroxylation of the piperideine-2-carboxylic acid and tautomerization of the produced 3-hydroxyl dihydropicolinic acid. Therefore, this study unveils the unusual assembly logic of 3-HPA and sheds light on the potential of engineering the 3-HPA pathway for generating novel pyridine-based building blocks. |
last changed |
2020/02/20 14:45 |
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