Christopher T. Walsh

TL;DR: It is concluded that the action of d-amino acid oxidase on the substrate results in the formation of an enzyme-bound enamine which then undergoes two competing reactions: (a) It is released to the medium and spontaneously ketonizes to form ketobutyrate, and (b) the β position of the enamine is protonated on the enzyme to form α-iminobutyric acid.

TL;DR: It is confirmed that myxovirescin undergoes two isoprenoid-like beta-alkylations during its biosynthesis, including an unprecedented beta-ethylation.

TL;DR: This work has identified a minimum set of enzymes needed for generation of the pacidamycin scaffold from amino acid and nucleoside monomers, highlighting a freestanding thiolation domain (PacH) as a key carrier component in the peptidyl chain assembly as well as aFreestanding condensation (C)domain (PacI) catalyzing the release of the assembled peptide by a nucleosides moiety.

TL;DR: Three thiophosphotyrosyl peptides have been prepared and act as substrates and competitive inhibitors of these PTPase catalytic domains and assess pY sequence context recognition by HPTPβ catalytic domain.

TL;DR: The conformational change induced by enolpyruvyl-UDP-N- acetylglucosamine binding to MurB results in the closure of the substrate-binding channel over the substrate.