How immune peptidases change specificity: cathepsin G gained tryptic function but lost efficiency during primate evolution.

Lost Efficiency during Primate Evolution Cathepsin G Gained Tryptic Function but How Immune Peptidases Change Specificity:

A Pulmonary Perspective on GASPIDs: Granule-Associated Serine Peptidases of Immune Defense.

Airways are protected from pathogens by forces allied with innate and adaptive immunity. Recent investigations establish critical defensive roles for leukocyte and mast cell serine-class peptidases garrisoned in membrane-bound organelles-here termed Granule-Associated Serine Peptidases of Immune Defense, or GASPIDs. Some better characterized GASPIDs include neutrophil elastase and cathepsin G (...

Structural Basis for Specificity of Propeptide-Enzyme Interaction in Barley C1A Cysteine Peptidases

C1A cysteine peptidases are synthesized as inactive proenzymes. Activation takes place by proteolysis cleaving off the inhibitory propeptide. The inhibitory capacity of propeptides from barley cathepsin L and B-like peptidases towards commercial and barley cathepsins has been characterized. Differences in selectivity have been found for propeptides from L-cathepsins against their cognate and no...

Computational investigation of conformational variability and allostery in cathepsin K and other related peptidases

Allosteric targeting is progressively gaining ground as a strategy in drug design. Its success, however, depends on our knowledge of the investigated system. In the case of the papain-like cysteine peptidase cathepsin K, a major obstacle in our understanding of allostery is represented by the lack of observable conformational change at the active site. This makes it difficult to understand how ...

Substrate specificity and inhibitor sensitivity of a Trypanosoma cruzi alkaline peptidase.

enzyme is a true cathepsin L. No enzyme with properties of cathepsin B were detected in T. cnrzi, although the enzyme described by Cazzulo and co-workers [3-51 has some features in common with cathepsin B. The enzyme that cleaves Ala-Ala-pNA is inhibited by E64, iodoacetic acid and leupeptin, but is not affected by inhibitors of serine, metalloor aspartic peptidases. It does not release p-nitro...