Transition state analysis of Pyranose 2-Oxidase from Peniophora sp.
Significant interest has been aroused for the use of pyranose 2-oxidase (P2Ox) as a catalyst in biotechnological applications particularly in biofuel and food technology. Understanding the transition state of this enzyme offers greater possibility to improve the catalytic activity of this enzyme...
| Main Authors: | , , |
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| Format: | Conference or Workshop Item |
| Language: | English English English |
| Published: |
2013
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| Subjects: | |
| Online Access: | http://irep.iium.edu.my/34141/ http://irep.iium.edu.my/34141/5/ICBIOE_2013_Cover_Page_till_Table_of_contents.pdf http://irep.iium.edu.my/34141/1/TST_P2Ox_-_ICBioE2013_proceedings_paper_pp274-277-.pdf http://irep.iium.edu.my/34141/4/Brochure.pdf |
| Summary: | Significant interest has been aroused for the use of pyranose 2-oxidase (P2Ox) as a catalyst in
biotechnological applications particularly in biofuel and food technology. Understanding the
transition state of this enzyme offers greater possibility to improve the catalytic activity of this
enzyme and thus speeding the industrial processes. The main purpose of this study is to identify and
characterize the transition states for the catalytic reaction of P2Ox from white-rot fungus
Peniophora sp.. The complete path for the oxidation reaction catalyzed by P2Ox was investigated
using the PM7 semi-empirical method with MOZYME function as implemented in the MOPAC
2012 (Molecular Orbital PACkage) program. The results of this study was consistent with the
experimental method where appreciable conformational changes can be seen in the loop of residues
454-461 which was anticipated to be functions as a gatekeeper to allow the substrate to pass into
the active center.
Keywords: pyranose-2-oxidase, fungus, transition state, PM7, MOZYME |
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