TY  - THES
A1  - Picchi, Douglas Gatte
T1  - On the characterisation of biosynthetic pathways and functional metagenomic approaches of cyanobacterial peptides
Y1  - 2013
CY  - Potsdam
ER  - 
TY  - JOUR
A1  - Kehr, Jan-Christoph
A1  - Picchi, Douglas Gatte
A1  - Dittmann-Thünemann, Elke
T1  - Natural product biosyntheses in cyanobacteria a treasure trove of unique enzymes
JF  - Beilstein journal of organic chemistry
N2  - Cyanobacteria are prolific producers of natural products. Investigations into the biochemistry responsible for the formation of these compounds have revealed fascinating mechanisms that are not, or only rarely, found in other microorganisms. In this article, we survey the biosynthetic pathways of cyanobacteria isolated from freshwater, marine and terrestrial habitats. We especially emphasize modular nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) pathways and highlight the unique enzyme mechanisms that were elucidated or can be anticipated for the individual products. We further include ribosomal natural products and UV-absorbing pigments from cyanobacteria. Mechanistic insights obtained from the biochemical studies of cyanobacterial pathways can inspire the development of concepts for the design of bioactive compounds by synthetic-biology approaches in the future.
KW  - cyanobacteria
KW  - natural products
KW  - NRPS
KW  - PKS
KW  - ribosomal peptides
Y1  - 2011
U6  - https://doi.org/10.3762/bjoc.7.191
SN  - 1860-5397
VL  - 7
IS  - 2
SP  - 1622
EP  - 1635
PB  - Beilstein-Institut zur Förderung der Chemischen Wissenschaften
CY  - Frankfurt, Main
ER  - 
TY  - JOUR
A1  - Gatte-Picchi, Douglas
A1  - Weiz, Annika
A1  - Ishida, Keishi
A1  - Hertweck, Christian
A1  - Dittmann-Thünemann, Elke
T1  - Functional analysis of environmental DNA-derived microviridins provides new insights into the diversity of the tricyclic peptide family
JF  - Applied and environmental microbiology
N2  - Microviridins represent a unique family of ribosomally synthesized cage-like depsipeptides from cyanobacteria with potent protease-inhibitory activities. The natural diversity of these peptides is largely unexplored. Here, we describe two methodologies that were developed to functionally characterize cryptic microviridin gene clusters from metagenomic DNA. Environmental samples were collected and enriched from cyanobacterial freshwater blooms of different geographical origins containing predominantly Microcystis sp. Microviridins were produced either directly from fosmid clones or after insertion of environmental DNA-derived gene cassettes into a minimal expression platform in Escherichia coli. Three novel microviridin variants were isolated and tested against different serine-type proteases. The comparison of the bioactivity profiles of the new congeners allows deduction of further structure-function relationships for microviridins. Moreover, this study provides new insights into microviridin processing and gene cluster organization.
Y1  - 2014
U6  - https://doi.org/10.1128/AEM.03502-13
SN  - 0099-2240
SN  - 1098-5336
VL  - 80
IS  - 4
SP  - 1380
EP  - 1387
PB  - American Society for Microbiology
CY  - Washington
ER  -