EC Number   |
General Information |
Reference |
|---|
   3.4.22.2 | evolution |
all four major papain-like cysteine proteases (PLCPs) purified from papaya latex, including papain, chymopapain, glycyl endopeptidase and caricain, are grouped into the lineage-specific expansion branch in the subfamily III of papain-like cysteine proteases (PLCPs). Tandem duplications play the dominant role in affecting copy number of PLCPs in plants. Significant variations in size of the PLCP subfamilies among species may reflect genetic adaptation of plant species to different environments. The lineage-specific expansion of papaya PLCPs of subfamily III might have been promoted by the continuous reciprocal selective effects of herbivore attack and plant defense. Phylogenetic analysis, conserved domain identification, gene duplication analysis, and chromosomal distribution of PLCPs, overview |
753097 |
| 3.4.22.2 | metabolism |
papain-like cysteine proteases (PLCPs), a large group of cysteine proteases structurally related to papain, play important roles in plant development, senescence, and defense responses |
753097 |
| 3.4.22.2 | more |
adsorption properties of protein papain at the solid/liquid interfaces of different hydrophobicity (highly oriented pyrolytic graphite (HOPG), bare gold, CH3, OH, and COOH-terminated self-assembled monolayers on gold) are studied by a combined quartz crystal microbalance and atomic force microscopy techniques. Papain forms an incomplete monolayer at hydrophobic interfaces (HOPG and CH3-terminated substrate), whereas on more hydrophilic ones, a complete monolayer formation is always observed with either the onset of the formation of a second layer (bare gold substrate) or adsorption in a multilayer fashion, possibly a bilayer formation (OH-terminated substrate). The surface concentration and compact monolayer film thickness is much lower on the COOH-terminated substrate compared to other surfaces studied. This result is explained by partial dissociation of the interfacial COOH groups leading to additional electrostatic interactions between the positively charged protein domains and negatively charged carboxylate anions, as well as to local pH changes promoting protein denaturation |
752880 |
| 3.4.22.2 | physiological function |
papain displays a strong anti-angiogenic effect in VEGF activated HUVEC human umbilical vein endothelial cells in vitro |
733572 |
