Sandbox 37

Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. Papain Introduction File:Papaya.jpg Carica papaya Papain is a cysteine protease that is stable and active under a wide range of conditions. The enzyme present in the leaves, latex, roots, and fruit of the papaya plant (Carica papaya). The papain proteins are synthesized as inactive precursors that become active within two minutes of the plant being wounded and the latex is expelled. The enzyme was first studied and isolated in the 1960's. It has a 23.4kDa theoretical molecular weight and works at an optimum pH of 6-7 and optimum temperature of 65 degrees Celsius. Structure spinqualitylabelsall models Papain (9PAP) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Papain's three-dimensional structure is at 1.65 Angstrom resolution. It consists of one polypepetide chain that is made up of 212 amino acids residues. There are three disulfide bonds present in the enzyme that maintains the protein's structure. secondary structure hydrophobic residues polar residues ligands van der Waals interactions hydrogen bonds Mechanism File:Papain mechanism.jpg Mechanism of papain catalysis active site Function Inhibition inhibitor van der Waals hydrogen bonds References