what are 4 proteases?

Answer 1

Check out www.wikipedia.org.
Some typically used proteases include trypsin, chymotrypsin, pepsin, and elastase. They cleave the peptide bond near certain amino acids. Trypsin cleaves near arginine and lysine, chymotrypsin cleaves near aromatic amino acids (tyrosine, tryptophan, and phenylalanine), and pepsin cleaves near two of the aromatic a.a's (Phe and Tyr). Elastase cleaves near glycine, alanine, and valine.

The proteases listed above are specific proteases. If you want the six categories of proteases, they are named by the specific amino acid within the protease molecule's active site (the site on the protease that cleaves the protein). These include serine proteases, threonine proteases, cysteine proteases, aspartic acid proteases, metalloproteases, and glutamic acid proteases.

Answer 2

There are currently six classes of proteases:

* Serine proteases
* Threonine proteases
* Cysteine proteases
* Aspartic acid proteases (e. g., plasmepsin)
* Metalloproteases
* Glutamic acid proteases

the threonine and glutamic acid proteases were not described until 1995 and 2004, respectively. The mechanism used to cleave a peptide bond involves making an amino acid residue that has the character of a polarized peptide bond (serine, cysteine and threonine peptidases) or a water molecule (aspartic acid, metallo- and glutamic acid peptidases) nucleophilic so that it can attack the peptide carbonyl group. One way to make a nucleophile is by a catalytic triad, where a histidine residue is used to activate serine, cysteine or threonine as a nucleophile.

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Answer 3

Serine,Theronine, cytiscine and glutimic acid.