Sandbox 37
From Proteopedia
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==Structure== | ==Structure== | ||
<StructureSection load='9PAP' size='400' align='left' caption='Papain (9PAP)' scene=''></StructureSection> | <StructureSection load='9PAP' size='400' align='left' caption='Papain (9PAP)' scene=''></StructureSection> | ||
| - | [[Image:Ramachandran plot.JPG| right| thumb| Ramachandran plot of papain amino acid residues]] | ||
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 <scene name='Sandbox_37/Papain_disulfide_bonds/1'>disulfide bonds</scene> present in the enzyme that maintains the protein's structure. Papain consists of 25% alpha helices and 21% beta sheets within its <scene name='Sandbox_37/Papain_beta-alpha/1'>secondary structure</scene>. Alpha helices are shown in red and beta sheets are shown in green. The enzyme's structure has a mixture of <scene name='Sandbox_37/Papain_hydrophobic/7'>hydrophobic residues</scene> shown in yellow and hydrophilic residues shown in purple. This corresponds to the protein's <scene name='Sandbox_37/Papain_polar/1'>polar residues</scene> shown in orange and nonpolar residues shown in green. | 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 <scene name='Sandbox_37/Papain_disulfide_bonds/1'>disulfide bonds</scene> present in the enzyme that maintains the protein's structure. Papain consists of 25% alpha helices and 21% beta sheets within its <scene name='Sandbox_37/Papain_beta-alpha/1'>secondary structure</scene>. Alpha helices are shown in red and beta sheets are shown in green. The enzyme's structure has a mixture of <scene name='Sandbox_37/Papain_hydrophobic/7'>hydrophobic residues</scene> shown in yellow and hydrophilic residues shown in purple. This corresponds to the protein's <scene name='Sandbox_37/Papain_polar/1'>polar residues</scene> shown in orange and nonpolar residues shown in green. | ||
| + | [[Image:Ramachandran plot.JPG| right| thumb| Ramachandran plot of papain amino acid residues]] | ||
Revision as of 01:13, 14 November 2011
| 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. |
Contents |
Papain
Introduction
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).[1] The papain proteins are synthesized as inactive precursors that become active within two minutes of the plant being wounded and the latex is expelled.[2] The latex is dried and then purified to extract the active papain enzme. 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 60-70 degrees Celsius.
Structure
|
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 present in the enzyme that maintains the protein's structure. Papain consists of 25% alpha helices and 21% beta sheets within its . Alpha helices are shown in red and beta sheets are shown in green. The enzyme's structure has a mixture of shown in yellow and hydrophilic residues shown in purple. This corresponds to the protein's shown in orange and nonpolar residues shown in green.
Mechanism
Function
Inhibition
References
- ↑ http://www.britannica.com/EBchecked/topic/441803/papain
- ↑ http://www.worthington-biochem.com/pap/default.html
- ↑ http://www.pdb.org/pdb/explore/remediatedSequence.do?structureId=1POP¶ms.chainEntityStrategyStr=all
- ↑ http://en.wikipedia.org/wiki/Papain
- ↑ http://www.pdb.org/pdb/explore.do?structureId=9PAP
- ↑ http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html
