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Papain, also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) enzyme present in papaya (Carica papaya) and mountain papaya (Vasconcellea cundinamarcensis). It is the namesake member of the papain-like protease family.
Papain-like proteases share a common catalytic dyad active site featuring a cysteine amino acid residue that acts as a nucleophile. [1] The human genome encodes eleven cysteine cathepsins which have a broad range of physiological functions. [3] In some parasites papain-like proteases have roles in host invasion, such as cruzipain from ...
Recognition sequence: Sequence of DNA recognized by the enzyme and to which it specifically binds. Cut : Displays the cut site and pattern and products of the cut. The recognition sequence and the cut site usually match, but sometimes the cut site can be dozens of nucleotides away from the recognition site.
Recognition sequence: Sequence of DNA recognized by the enzyme and to which it specifically binds. Cut : Cutting site and DNA products of the cut. The recognition sequence and the cutting site usually match, but sometimes the cutting site can be dozens of nucleotides away from the recognition site [ 5 ] [ 6 ] .
The enzyme papain can be used to cleave an immunoglobulin monomer into two Fab fragments and an Fc fragment. Conversely, the enzyme pepsin cleaves below the hinge region, so the result instead is a F(ab') 2 fragment and a pFc' fragment.
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Recombination between two DNA sites begins by the recognition and binding of these sites – one site on each of two separate double-stranded DNA molecules, or at least two distant segments of the same molecule – by the recombinase enzyme. This is followed by synapsis, i.e. bringing the sites together to form the synaptic complex.