James Strand

TL;DR: Steady state kinetics shows that human AMCase has "low" intrinsic transglycosidase activity, which leads to the observation of apparent substrate inhibition, which may provide a mechanism in vivo for feedback regulation of the chitinase activity of human AM case.

TL;DR: The novel structure of the AMCase catalytic domain, both in the apo form and in complex with the inhibitor methylallosamidin, determined to high resolution by X‐ray crystallography provides a structural basis for understanding some of the unique characteristics of this enzyme, including the low pH optimum and the preference for the β‐anomer of the substrate.

TL;DR: Small molecule inhibitors of AMCase were identified using a combination of high-throughput screening, fragment screening, and virtual screening techniques and characterized by enzyme inhibition and NMR and Biacore binding experiments and revealed that the larger more potent HTS hits spanned from the active site pocket to a hydrophobic pocket.

TL;DR: In this article, high resolution structures of acidic mammalian chitinase (AMCase) were described and the structures enable selection of, and structure-based rational drug design of, agents that modulate, e.g., antagonize, AMCase activity.