Carol A. Fierke

TL;DR: These studies demonstrate that the chemical nature of the direct ligands and the structure of the surrounding hydrogen bond network are crucial for both the activity of carbonic anhydrase and the metal ion affinity of the zinc-binding site.

TL;DR: A kinetic scheme is presented for Escherichia coli dihydrofolate reductase that predicts steady-state kinetic parameters and full time course kinetics under a variety of substrate concentrations and pHs and accounts for the apparent pKa =8.4 observed in the steady state as due to a change in the rate-determining step from product release at low pH to hydride transfer above pH 8.4.

TL;DR: This work quantitatively image intracellular exchangeable zinc in an ordinary resting cell culture line (PC-12), using an excitation ratiometric fluorescent biosensor based on carbonic anhydrase (CA), and indicates that the resting concentration is approximately 5-10 pM in cytoplasm and nucleus.

TL;DR: Pulse‐chase experiments and in vitro assays with purified components showed that FtsH, the AAA‐type membrane‐bound metalloprotease, degrades the deacetylase, which indicates that the biosynthesis of phospholipids and the lipid A moiety of lipopolysaccharide, both of which derive their fatty acyl chains from the same R‐3‐hydroxyacyl‐ACP pool, is regulated by FTSH.