The first structure of a bacteriophage-encoded S-adenosyl methionine degrading enzyme was solved and demonstrated to catalyze a unimolecular lyase reaction occurring at the domain interface of a trimeric structure.

A novel dimethylsulfoniopropionate lyase was identified, which catalyzes dimethyl sulfide releasing by a new mechanism and is found in several bacterial lineages, revealing its important roles in global sulfur cycling.

Small molecule inhibitors of gut microbial choline trimethylamine lyase activity protect against obesity.

Upon deletion of threonine deaminases, biosynthesis of isoleucine is rescued by two promiscuous reactions, one emerges under aerobic conditions and the other is naturally active under anaerobic conditions.

Degradation products of polysaccharides trigger partial population dispersal and alter cellular metabolism, shaping the marine biomass decomposition by foraging bacteria.

Structural and biochemical studies explain the topoisomerase V DNA relaxation mechanism by showing that it adopts an unusual conformation when bound to DNA that exposes the active site.

Co-evolving residue pairs in the different components of a protein complex almost always make contact across the protein–protein interface, thus providing powerful restraints for the modeling of protein complexes.

Metabolic flux analysis, biochemistry assays, and functional confirmation in mice show that the ubiquitination and degradation of ATP-citrate lyase (ACLY) mediated by CUL3-KLHL25 promotes the switch from fatty acid synthesis to fatty acid oxidation for iTreg differentiation.

The gut microbe-derived metabolite trimethylamine (TMA) is elevated in patients with alcohol-associated hepatitis and inhibition of the gut microbial enzymes that produce TMA may serve as a tractable therapeutic strategy for the treatment of ethanol-induced liver injury.