Proteases in a sentence

Acid proteases secreted into the stomach (such as pepsin ) and serine proteases present in duodenum ( trypsin and chymotrypsin ) enable us to digest the protein in food.

Furthermore, it provides lipases, proteases, oxidoreductases, and carbohydrases.

Instead of DNA-based systems, the researchers built their decision-making circuit with proteins, de novo protein heterodimers and engineered proteases.

After complement proteins initially bind to the microbe, they activate their protease activity, which in turn activates other complement proteases, and so on.

A good example is the blood clotting cascade whereby an initial event triggers a cascade of sequential proteolytic activation of many specific proteases, resulting in blood coagulation.

As an example, one may consider proteases (enzymes that aid digestion by causing hydrolysis of peptide bonds in proteins ).

A variety of proteases are used medically both for their native function (e.g. controlling blood clotting) or for completely artificial functions (e.g. for the targeted degradation of pathogenic proteins).

By complex cooperative action the proteases may proceed as cascade reactions, which result in rapid and efficient amplification of an organism's response to a physiological signal.

Caspases are proteins that are highly conserved, cysteine-dependent aspartate-specific proteases.

Catalysis Catalysis is achieved by one of two mechanisms: *Aspartic, glutamic and metallo- proteases activate a water molecule which performs a nucleophilic attack on the peptide bond to hydrolyse it.

Cooking or canning denatures and deactivates the proteases, so canned pineapple, for example, works fine in a gelatin dessert.

Degradation and autolysis Proteases, being themselves proteins, are cleaved by other protease molecules, sometimes of the same variety.

Highly specific proteases such as TEV protease and thrombin are commonly used to cleave fusion proteins and affinity tags in a controlled fashion.

However, proteases do not catalyse the hydrolysis of all kinds of proteins.

Like many proteases, chymotrypsin will also hydrolyse amide bonds in vitro, a virtue that enabled the use of substrate analogs such as N-acetyl-L-phenylalanine p-nitrophenyl amide for enzyme assays.

Plants Plant genomes encode hundreds of proteases, largely of unknown function.

Promiscuous proteases typically bind to a single amino acid on the substrate and so only have specificity for that residue.

Proteases are the most commonly used enzymes in leather production.

Proteases can either break specific peptide bonds (limited proteolysis), depending on the amino acid sequence of a protein, or break down a complete peptide to amino acids (unlimited proteolysis).

Some proteases are less active after autolysis (e.g. TEV protease ) whilst others are more active (e.g. trypsinogen ).