Brian O. Bachmann
@brianobachmann.bsky.social
1K followers
720 following
99 posts
Prof. Chemical Biology, PI the Vanderbilt Laboratory for Biosynthetic Studies. Posting natural product tilted human chemical biology, biosynthesis, synthetic biology, and discovery. He/him.
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Reposted by Brian O. Bachmann
Reposted by Brian O. Bachmann
Reposted by Brian O. Bachmann
Reposted by Brian O. Bachmann
Reposted by Brian O. Bachmann
Rauf Salamzade
@raufs.bsky.social
· Feb 24
Context matters: assessing the impacts of genomic background and ecology on microbial biosynthetic gene cluster evolution | mSystems
Microbial secondary metabolites are compounds produced by bacteria and fungi that
are not required for their replication and unconditional survival (1, 2). While they are thus not expected to be unive...
journals.asm.org
Reposted by Brian O. Bachmann
ChemKritzer
@chemkritzer.bsky.social
· Feb 19
Reposted by Brian O. Bachmann
Reposted by Brian O. Bachmann
Avena Ross
@avenaross.bsky.social
· Jan 29
Activation of Primary C–H Bonds in Oxidative Cyclizations of Tambjamines Catalyzed by Rieske Oxygenases TamC and PtTamC
Tambjamines are complex bipyrrole-containing natural products that possess promising bioactive properties. Although Pseudoalteromonas citrea is known to produce both cyclic tambjamine MYP1 and the linear precursor (YP1), the biosynthetic machinery used to catalyze the site-selective oxidative carbocyclization at the unactivated 1° carbon of YP1 has remained unclear. Here, we demonstrate that a three-component Rieske system consisting of an oxygenase (TamC) and two redox partner proteins is responsible for this unprecedented activity on YP1 and potentially, a non-native substrate (BE-18591). We also show that a homologous oxidase from Pseudoalteromonas tunicata (PtTamC) can function together with the partner proteins from P. citrea to process both YP1 and BE-18591. These reactions represent the first Rieske oxygenase-catalyzed activations of C–H bonds at 1° carbons, resulting in carbon–carbon bond formation. The use of TamC and PtTamC to potentially generate the new-to-nature cyclic analogue of BE-18591 suggests the enormous biocatalytic potential of these Rieske systems to facilitate late-stage oxidative cyclizations at terminal C(sp3)–H bonds.
pubs.acs.org
Reposted by Brian O. Bachmann
Yi Tang
@yitangucla.bsky.social
· Jan 29
Copper-dependent halogenase catalyses unactivated C−H bond functionalization - Nature
A halogenase enzyme uses the copper in its active site to catalyse iterative chlorinations on multiple unactivated carbon−hydrogen bonds, enabling carbon−hydrogen functionalization that is not achieva...
www.nature.com
Reposted by Brian O. Bachmann
Ran Blekhman
@blekhman.bsky.social
· Jan 22
Integration of 168,000 samples reveals global patterns of the human gut microbiome
The Human Microbiome Compendium is a unified database of publicly available human
gut microbiome 16S samples, built with the integrated data from hundreds of independent
projects. The compendium is us...
www.cell.com
Reposted by Brian O. Bachmann
Nigel Mouncey
@nigelmouncey.bsky.social
· Jan 17
Microbial secondary metabolites: advancements to accelerate discovery towards application
Nature Reviews Microbiology - In this Review, Dinglasan and colleagues explore innovations that facilitate rapid microbial secondary metabolite discovery, focusing on recent techniques for the...
rdcu.be