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Proteases are enzymes that hydrolyse peptide bonds between the residues that conform a protein. In every hydrolysis a water molecule is released. In every hydrolysis a water molecule is released. Specifically, a cysteine protease is an enzyme which breaks the peptide bond by using the thiol group of a cysteine residue as the nucleophile.
The enzyme is deacylated by a water molecule and releases the carboxy terminal portion of the peptide. In immunology, papain is known to cleave the Fc (crystallisable) portion of immunoglobulins (antibodies) from the Fab (antigen-binding) portion. Papain is a relatively heat-resistant enzyme, with an optimal temperature range of 60 to 70 °C. [9]
Glycyl endopeptidase (EC 3.4.22.25, papaya peptidase B, papaya proteinase IV, glycine-specific proteinase, ... This enzyme catalyses the following chemical reaction.
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[3] [10] [9] Many papain-like protease enzymes function as monomers, though a few, such as cathepsin C (Dipeptidyl-peptidase I), are homotetramers. The mature monomer structure is characteristically divided into two lobes or subdomains, known as the L-domain ( N-terminal ) and the R-domain ( C-terminal ), where the active site is located ...
Caricain can be assayed with Bz-ArgkNHPhNO2, kcat/Km being 187 M21 s21 at pH 6.8 and 40˚C. More sensitive substrates may employ a fluorometric leaving group, kcat/Km for the hydrolysis of Z-Phe-ArgkNHMec being 1.06 3 106 M21 s21 (pH 6.8, 40˚C). [5] The enzyme exhibits a broad pH-activity profile, with the optimum near 7.0.
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