proteaze

Proteaze is a hypothetical protease enzyme used in education and illustrative case studies to demonstrate how proteolysis works. In many classroom and reference materials, Proteaze is described as a serine protease with an active site that operates via a catalytic triad to hydrolyze peptide bonds in proteins. The model emphasizes a general mechanism shared with many proteases, involving nucleophilic attack on the carbonyl carbon of the peptide bond and formation of a peptide fragment and a cleaved partner.

Proteolytic specificity: Proteaze is depicted as having broad substrate tolerance, cleaving after a range of amino acids, with contextual preferences depending on neighboring residues and the substrate’s structure. This flexibility makes Proteaze a convenient teaching tool for illustrating concepts such as proteolytic specificity, enzyme kinetics, and the effect of pH and temperature on activity.

Production and use: In educational contexts, Proteaze is often described as being produced recombinantly in simple microbial hosts or supplied as a purified enzyme in teaching kits. It is used in demonstrations of proteolysis in gel assays, peptide mapping, or sample preparation workflows to model protease behavior without handling hazardous materials.

Limitations and note: Proteaze is a fictional construct and not a verified natural or engineered enzyme. For real experiments, researchers rely on established proteases such as trypsin, chymotrypsin, or commercial proteases with documented properties.

References: See protease, serine protease, enzyme specificity.