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

In nonribosomal peptide synthetase (NRPS) research, expanding our understanding of the relationship between active-site amino acid residues in adenylation (A) domains and their adenylation activity and substrate specificity remains essential, as detailed biochemical characterization is still limited. In this study, we...

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

Methanogenic archaea harbor diverse enzymes that support their survival in extreme environments and play key roles in global carbon cycling. The C39 peptidase family, known for cleaving peptide substrates, now gains functional expansion through A0A126R2S0, a novel enzyme that shares structural homology with C39 peptida...

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

It is common for bacteriophages to encode proteins that are strongly inhibitory to growth of the bacterial host, and about 10% of mycobacteriophage-encoded proteins have this property. Adephagia is a Cluster K1 mycobacteriophage and prior cloning and expression of 66 Adephagia non-structural genes identified 14 that ar...

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