Fabclavine biosynthesis in X. szentirmaii: shortened derivatives and characterization of the thioester reductase FclG and the condensation domain-like protein FclL.

Abstract:

:Fabclavines, unusual peptide-polyketide-polyamine hybrids, show broad-spectrum bioactivity against a variety of different organism like Gram-positive and -negative bacteria, fungi and protozoa. We elucidated the biosynthesis of these NRPS-PKS hybrids in Xenorhabdus szentirmaii by deletion of most genes encoded in the fabclavine BGC and subsequent analysis of produced fabclavine or polyamine intermediates. Thereby, we identified shortened fabclavines similar to the bioactive zeamines. Furthermore, we analyzed the thioester reductase FclG and the free-standing condensation domain-like protein FclL in detail and observed low substrate specificity for both enzymes.

authors

Wenski SL,Kolbert D,Grammbitter GLC,Bode HB

doi

10.1007/s10295-018-02124-8

subject

Has Abstract

pub_date

2019-03-01 00:00:00

pages

565-572

issue

3-4

eissn

1367-5435

issn

1476-5535

pii

10.1007/s10295-018-02124-8

journal_volume

46

pub_type

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