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Issue 3, 2019
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In vitro reconstitution of the biosynthetic pathway of 3-hydroxypicolinic acid

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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.

Graphical abstract: In vitro reconstitution of the biosynthetic pathway of 3-hydroxypicolinic acid

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Publication details

The article was received on 28 Nov 2018, accepted on 10 Dec 2018 and first published on 10 Dec 2018


Article type: Communication
DOI: 10.1039/C8OB02972E
Org. Biomol. Chem., 2019,17, 454-460

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    In vitro reconstitution of the biosynthetic pathway of 3-hydroxypicolinic acid

    X. Yun, Q. Zhang, M. Lv, H. Deng, Z. Deng and Y. Yu, Org. Biomol. Chem., 2019, 17, 454
    DOI: 10.1039/C8OB02972E

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