Christopher T. Walsh

TL;DR: This article attempts to answer several basic questions of or comments on thiolase substrate specificity, identified of the active site cysteine involved in acetyl enzyme formation in the first half reaction, identification of theactive site basic residue responsible for deprotonation of the second acetyl-CoA molecule, and the energy profile of the forward and reverse reactions.

TL;DR: Results suggest a strong resemblance of catalysis by the EntF C domain to chloramphenicol acetyltransferase, including an active site organized by an arginine-aspartate salt bridge, a key histidine acting as a general base, and an asparagine instead of a serine stabilizing the proposed tetrahedral intermediate by hydrogen bonding.

TL;DR: The apoenzyme had no affinity to DNA but did regain its specific binding to thymine dimer containing DNA upon binding stoichiometrically to FAD or 5-deazaFAD and showed high-affinity binding to apophotolyase.

TL;DR: This work has shown how posttranslational modifications downstream of leader peptide regions that convert up to 10 serine, threonine, and cysteine residues, side chains and peptide backbones, into oxazoles, thiazoles, and pyridine rings can be augmented in microbial proteins.