Sandbox 37: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
==Introduction== | ==Introduction== | ||
[[Image:Papaya.jpg | right| thumb| ''Carica papaya'']] | [[Image:Papaya.jpg | right| thumb| ''Carica papaya'']] | ||
<scene name='Sandbox_37/Main_scene/1'>Papain</scene> 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'').<ref>http://www.britannica.com/EBchecked/topic/441803/papain</ref> The papain proteins are synthesized as inactive precursors that become active within two minutes of the plant being wounded and the latex is expelled.<ref>http://www.worthington-biochem.com/pap/default.html</ref> | <scene name='Sandbox_37/Main_scene/1'>Papain</scene> 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'').<ref>http://www.britannica.com/EBchecked/topic/441803/papain</ref> The papain proteins are synthesized as inactive precursors that become active within two minutes of the plant being wounded and the latex is expelled.<ref>http://www.worthington-biochem.com/pap/default.html</ref> 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== | ==Structure== | ||
<StructureSection load='9PAP' size='400' align='left' caption='Papain (9PAP)' scene=''></StructureSection> Papain 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. | <StructureSection load='9PAP' size='400' align='left' caption='Papain (9PAP)' scene=''></StructureSection> 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. | ||
<scene name='Sandbox_37/Papain_beta-alpha/1'>secondary structure</scene> | <scene name='Sandbox_37/Papain_beta-alpha/1'>secondary structure</scene> | ||
Revision as of 00:44, 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.
PapainIntroductionPapain 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 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
MechanismFunctionInhibitionReferences
|