Molecular dynamics of serine proteases.

Serine proteases: an ab initio molecular dynamics study.

In serine proteases (SPs), the H-bond between His57 and Asp102 and that between Gly193 and the transition state intermediate play a crucial role in enzymatic function. To shed light on the nature of these interactions, we have carried out ab initio molecular dynamics simulations on complexes representing adducts between the reaction intermediate and elastase (one protein belonging to the SP fam...

Molecular cloning of serine proteases from elapid snake venoms.

Serine proteases are widely distributed in viperid snake venoms, but rare in elapid snake venoms. Previously, we have identified a fibrinogenolytic enzyme termed OhS1 from the venom of Ophiophagus hannah. The results indicated that OhS1 might be a serine protease, but there was no structural evidence previously. In the present study, the primary structure of OhS1 was determined by protein seque...

Plant serine proteases: biochemical, physiological and molecular features.

In the latest two decades, the interest received by plant proteases has been on the rise. Serine proteases (EC 3.4.21)-in particular those from cucurbits, cereals and trees-share indeed a number of biochemical and physiological features, that may prove useful toward understanding of several mechanisms at the subcellular level. This critical review focuses on the characterization of most plant s...

Serine Proteases of Parasitic Helminths

Serine proteases form one of the most important families of enzymes and perform significant functions in a broad range of biological processes, such as intra- and extracellular protein metabolism, digestion, blood coagulation, regulation of development, and fertilization. A number of serine proteases have been identified in parasitic helminths that have putative roles in parasite development an...

Detection of the Keratinolytic Activity of Agriculture and Mount Barker Strain Dermatophilus congolensis Serine Proteases.