Identification of key amino acid residues governing substrate-entry, catalysis and dimerization in 1-naphthol-2-hydroxylase from Pseudomonas sp. C5pp.

Unexpected roles of aromatic ring-cleaving dioxygenases in oxygen-heterocycle degradation: Functional diversity, gene redundancy, and ecological implications.

This work demonstrates that classical aromatic ring-cleaving dioxygenases mediate the cellular cleavage of 2-hydroxytetrahydrofuran (2-OH THF), a key intermediate in THF metabolism, to yield 4-hydroxybutyric acid (GHB), and establishes a novel catalytic route for cyclic ether degradation in aquatic systems.

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.

Substrate-pocket reshaping of an (R)-selective transaminase enables efficient asymmetric synthesis of (R)-3-amino-1-butanol.

(R)-Selective ω-transaminases are valuable biocatalysts for the synthesis of chiral amines and pharmaceutical intermediates, but their practical application is often limited by insufficient catalytic efficiency, poor operational stability and unfavorable reaction equilibrium. Here, an Actinomycete-derived (R)-selective...

Biosynthesis of YM-216391 Unveils a Bifunctional α-Ketoglutarate-Dependent Enzyme Catalyzes Hydroxylation and Epimerization in RiPPs.

The RiPP-modifying enzyme YmI is reported, a bifunctional Fe/αKGD that catalyzes Cβ-hydroxylation of Phe19 and Cα-epimerization of Ile20 on the precursor peptide YmA toward the formation of YM-216391, unveiling an unprecedented mechanism and novel bifunctionality, markedly expanding the reaction landscape for αKG-depen...

Mechanistic Roles of Conserved Active-Site Residues in OXA-48 Carbapenem Hydrolysis.

Results support a model in which conserved hydrophobic active-site residues optimize the geometric and electrostatic environment required for efficient carbapenem deacylation and turnover, and provide mechanistic insight into OXA-48 catalysis that may be exploited to design inhibitors targeting the enzyme.

[Directed evolution of amine dehydrogenase for the catalytic resolution of (1R,5S)-3-ethylbicyclo [3.2.0] hept-3-en-6-one, a chiral intermediate of mirogabalin].