Transferases articles from across Nature Portfolio

Coactivator-associated arginine methyltransferase 1 (CARM1) is an important target in hematologic malignancies. In this work, the authors show that the hyperactivation of Janus kinase 2 (JAK2) by the V617F mutation phosphorylates CARM1 which regulates its methyltransferase activity and alters its target specificity.

Here, the authors structurally and functionally characterise DltB, a member of the Membrane-Bound O-AcylTransferase (MBOAT) superfamily responsible for D-alanine incorporation in the cell wall of gram-positive bacteria.

Phosphoinositide 3-kinase γ plays critical roles in neutrophil chemotaxis and cancer metastasis. Here, using cryo-EM and functional studies, the authors reveal how two molecules of a key activator, Gβγ, bind to and alter the conformation of the enzyme.

Here the authors report a strategy to directly capture substrates of lysine-modifying enzymes via post-translational modification (PTM)-acceptor residue crosslinking in living cells, enabling global profiling of substrates of PTM-enzymes and validation of PTM-sites in a straightforward manner.

Heparan sulfate biosynthesis is a complex process involving multiple reactions that extend and modify the polysaccharide. Here, the authors resolve structures of NDST1, responsible for the critical N-sulfoglucosamine modification of heparan sulfate.

Acyltransferase activity of the enzyme bile salt hydrolase is identified and shown to mediate microbial bile acid conjugation, diversifying the bile acid pool and expanding their role in gut physiology.

Protein lysine methylation plays important biological roles but its experimental characterization is limited by the lack of suitable mimetics of methylated and unmethylated lysine among the natural amino acids. Here, we summarize the consequent challenges and discuss alternative approaches for biochemical and cellular lysine methylation studies.

More than 35 years ago, telomerase activity was discovered by Elizabeth H. Blackburn and Carol W. Greider. Today, this enzyme is a promising approach to curing some age-related diseases as well as cancer, but it took time for telomerase to be in the spotlight.

García Saura et al. report a new tool, MacroGreen, to detect ADP-ribosylation by GFP fluorescence in a microplate reader, or in cells by microscopy. With superior affinity and reduced ADP-ribosyl hydrolase activity, MacroGreen is an easy to produce and suitable tool for rapid detection of ADP-ribosylated proteins in vitro without a need for specialist reagents and time-consuming methods.

Polyketide synthases are multi-domain enzymes that catalyse the construction of many bioactive natural products. Now, some of the inefficiencies and limitations of these systems have been solved by designing an artificial pathway for carbon–carbon bond formation via iterative rounds of non-decarboxylative thio-Claisen reactions.

A strategy using pressure was devised to structurally identify conformational transitions in protein ensembles, allowing the rational prediction of mutations that induce pressure-driven enzyme activation. These results highlight the power of flexibility–function analyses in protein engineering design and applications.

S-adenosylmethionine (SAM)-dependent methyltransferase enzymes have significant synthetic potential, but their utility as biocatalysts has been limited by the availability of SAM. An elegant and simple method addressing this long-standing problem has now been developed using a halide methyltransferase (HMT) enzyme for SAM regeneration in vitro.