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Issue 26, 2017
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Enzymatic competition and cooperation branch the caerulomycin biosynthetic pathway toward different 2,2′-bipyridine members

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Abstract

In this study, we characterized CaeB6 as a selective hydroxylase and CaeG1 as an O-methyltransferase in the biosynthesis of the 2,2′-bipyridine natural products caerulomycins (CAEs). The C3-hydroxylation activity of CaeB6 competes with the C4-O-methylation activity of CaeG1 and thereby branches the CAE pathway from a common C4-O-demethylated 2,2′-bipyridine intermediate. CaeG1-catalyzed C4-O-methylation leads to a main route that produces the major product CAE-A in Actinoalloteichus cyanogriseus NRRL B-2194. In contrast, CaeB6-catalyzed C3-hydroxylation results in a shunt route in which CaeG1 causes C4-O-methylation and subsequent C3-O-methylation to produce a series of minor CAE products. These findings provide new insights into the biosynthetic pathway of CAEs and a synthetic biology strategy for the selective functionalization of the 2,2′-bipyridine core.

Graphical abstract: Enzymatic competition and cooperation branch the caerulomycin biosynthetic pathway toward different 2,2′-bipyridine members

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Publication details

The article was received on 25 May 2017, accepted on 16 Jun 2017 and first published on 16 Jun 2017


Article type: Communication
DOI: 10.1039/C7OB01284E
Citation: Org. Biomol. Chem., 2017,15, 5472-5475
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    Enzymatic competition and cooperation branch the caerulomycin biosynthetic pathway toward different 2,2′-bipyridine members

    M. Chen, Y. Zhang, Y. Du, Q. Zhao, Q. Zhang, J. Wu and W. Liu, Org. Biomol. Chem., 2017, 15, 5472
    DOI: 10.1039/C7OB01284E

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