Sandbox Reserved 1477: Difference between revisions
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==Introduction== | ==Introduction== | ||
The topic is going to be the structural study of the enzyme '''glucose oxidase''' from aspergillus niger. It is not an enzyme from human body. Instead, it is found in the cells of fungus. | The topic is going to be the structural study of the enzyme '''glucose oxidase''' from aspergillus niger. It is not an enzyme from human body. Instead, it is found in the cells of fungus. These types of enzymes catalysts the oxidation of beta-D-glucose to δ-gluconolactone and H2O2 (which is not a reaction happening in human body) <ref>PMID:10216293</ref>. I don't think there is any medical application for this certain enzyme since it is not even an enzyme from human body. The only possible medical application might be producing medicines with this type of reaction. | ||
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Two PDB codes mentioned by the essay, 1cf3 and 1gpe, which are two glucose oxidases from different organisms. They have exactly the same types of ligands, which might mean there is some functional issue with the present of those ligands, especially the dimer of beta-D-glucose (MAN). This essay was published back to 1999, which is fairly old in the scale of proteomic. | |||
== Function == | == Function == | ||
[[Image:MAN and BMA.png]] | [[Image:MAN and BMA.png]] | ||
Cyan part is a dimer of MAN (which is one of the reactants of the reaction this enzyme catalysts), magenta part is a BMA molecule. | Cyan part is a dimer of MAN (which is one of the reactants of the reaction this enzyme catalysts), magenta part is a BMA molecule. | ||
<scene name='80/800656/Asn89/1'> Residue ASN89</scene> | |||
== Energetic == | == Energetic == | ||
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<Structure load='1cf3' size='350' frame='true' align='right' caption='The glucose oxidase from Aspergillus Niger (PDB#:1cf3)' scene='Insert optional scene name here' /> | <Structure load='1cf3' size='350' frame='true' align='right' caption='The glucose oxidase from Aspergillus Niger (PDB#:1cf3)' scene='Insert optional scene name here' /> | ||
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
The structure of this enzyme contains only one chain with 4 different types of ligands. This is a 583-residue-long protein with the molecular weight of about 65.8kDa. The structure is tested by X-ray diffraction for the certain PDB entry with the code 1cf3. X-ray diffraction gives the information of the whole protein sequence (if the resolution of the instrument is high enough), which makes it better than any other methods with non-100% sequence courage. | |||
Another glucose oxidase also tested with X-ray diffraction method in the same essay from Penicillium Amagasakiense has two identical chains. As mentioned, they have exactly the same ligands, which actually make sense since they have the same function. | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
