A Single Substitution of Valine to Glutamic Acid in the Omega-Like Loop Introduces a Penicillinase-Like Activity in MSMEG_6194 by Compromising its Role as DD-Carboxypeptidase

Mutation-induced heterogeneity of the β7-β8 loop of the Staphylococcus aureus class A sortase leading to enhanced catalytic efficiency characterized by NMR and enzyme kinetics

NMR data, in combination with enzymatic assays using active variants confirmed differences in the active, apo states of these enzymes, and provided additional atomic detail regarding the importance of the P94 residue in saSrtA substrate recognition.

Identification of Key Amino Acid Residues in the Adenylation Domains of Polymyxin Synthetase Responsible for l‑Threonine Adenylation in Paenibacillus polymyxa NBRC3020

This study investigated two l-threonine (l-Thr)-specific A domains from the NRPS responsible for polymyxin D biosynthesis in Paenibacillus polymyxa NBRC 3020, and identified three residues within the 10-amino-acid Stachelhaus codePhe, Met, and His as key determinants of l-Thr side-chain recognition.

A C39-like protein from methanogenic archaea: structural insights and functional divergence in β-galactose analogue degradation

These findings expand the functional repertoire of the C39 peptidase superfamily, suggest an evolutionary connection between peptidases and glycosidases, and establish A0A126R2S0 as a candidate biocatalyst for β-galactoside processing.

Mycobacteriophage Adephagia gp48 inhibits essential host cell wall biosynthesis enzyme mannose-1-phosphate guanylyltransferase

It is shown that gp48 encoded by mycobacteriophage Adephagia is toxic when overexpressed in Mycobacterium smegmatis and Mycobacterium abscessus and the toxicity results from gp48 interaction with the host mannose-1-phosphate guanylyltransferase (Mpg) enzyme.

Structural insights into a putative BLF1-like deamidase from Methylomonas sp. Kb3.

Structural features suggest that the Methylomonas protein that is identified may act as a BLF1-like deamidase but against a currently unknown target, and that other bacterial proteins with similar sequence fingerprints could play important roles in broader bacterial biology.

Energetic coupling of an active site residue in penicillin-binding protein 2 from Neisseria gonorrhoeae with a resistance-associated conformational switch in the β3-β4 loop