Extension of polyphenolics by CWPO-C peroxidase mutant containing radical-robust surface active site.
Identifieur interne : 002442 ( Main/Curation ); précédent : 002441; suivant : 002443Extension of polyphenolics by CWPO-C peroxidase mutant containing radical-robust surface active site.
Auteurs : L T Mai Pham ; S Jin Kim ; U Suk Ahn ; J Weon Choi ; B Keun Song ; Y Hwan KimSource :
- Applied biochemistry and biotechnology [ 1559-0291 ] ; 2014.
Descripteurs français
- KwdFr :
- Antioxydants (métabolisme), Biocatalyse (MeSH), Cations (MeSH), Catéchine (composition chimique), Catéchine (métabolisme), Chromatographie sur gel (MeSH), Cinétique (MeSH), Dimérisation (MeSH), Domaine catalytique (MeSH), Mutation (génétique), Myeloperoxidase (métabolisme), Oxydoréduction (MeSH), Paroi cellulaire (enzymologie), Phénols (composition chimique), Phénols (métabolisme), Polymérisation (MeSH), Polyphénols (métabolisme), Populus (enzymologie), Radicaux libres (métabolisme), Similitude structurale de protéines (MeSH), Simulation de docking moléculaire (MeSH), Spectrophotométrie (MeSH), Stabilité enzymatique (MeSH), Thermodynamique (MeSH).
- MESH :
- composition chimique : Catéchine, Phénols.
- enzymologie : Paroi cellulaire, Populus.
- génétique : Mutation.
- métabolisme : Antioxydants, Catéchine, Myeloperoxidase, Phénols, Polyphénols, Radicaux libres.
- Biocatalyse, Cations, Chromatographie sur gel, Cinétique, Dimérisation, Domaine catalytique, Oxydoréduction, Polymérisation, Similitude structurale de protéines, Simulation de docking moléculaire, Spectrophotométrie, Stabilité enzymatique, Thermodynamique.
English descriptors
- KwdEn :
- Antioxidants (metabolism), Biocatalysis (MeSH), Catalytic Domain (MeSH), Catechin (chemistry), Catechin (metabolism), Cations (MeSH), Cell Wall (enzymology), Chromatography, Gel (MeSH), Dimerization (MeSH), Enzyme Stability (MeSH), Free Radicals (metabolism), Kinetics (MeSH), Molecular Docking Simulation (MeSH), Mutation (genetics), Oxidation-Reduction (MeSH), Peroxidase (metabolism), Phenols (chemistry), Phenols (metabolism), Polymerization (MeSH), Polyphenols (metabolism), Populus (enzymology), Spectrophotometry (MeSH), Structural Homology, Protein (MeSH), Thermodynamics (MeSH).
- MESH :
- chemical , chemistry : Catechin, Phenols.
- chemical , metabolism : Antioxidants, Catechin, Free Radicals, Peroxidase, Phenols, Polyphenols.
- enzymology : Cell Wall, Populus.
- genetics : Mutation.
- Biocatalysis, Catalytic Domain, Cations, Chromatography, Gel, Dimerization, Enzyme Stability, Kinetics, Molecular Docking Simulation, Oxidation-Reduction, Polymerization, Spectrophotometry, Structural Homology, Protein, Thermodynamics.
Abstract
Expressed as insoluble forms in Escherichia coli, native cationic cell wall peroxidase (CWPO-C) from the poplar tree and mutant variants were successfully reactivated via refolding experiments and used to elucidate the previously presumed existence of an electron transfer (ET) pathway in the CWPO-C structure. Their catalytic properties were fully characterized through various analyses including steady-state kinetic, direct oxidation of lignin macromolecules and their respective stabilities during the polymerization reactions. The analysis results proved that the 74th residue on the CWPO-C surface plays an important role in catalyzing the macromolecules via supposed ET mechanism. By comparing the residual activities of wild-type CWPO-C and mutant 74W CWPO-C after 3 min, mutation of tyrosine 74 residue to tryptophan increased the radical resistance of peroxidase up to ten times dramatically while maintaining its capability to oxidize lignin macromolecules. Furthermore, extension of poly(catechin) as well as lignin macromolecules with CWPO-C Y74W mutant clearly showed that this radical-resistant peroxidase mutant can increase the molecular weight of various kinds of polyphenolics by using surface-located active site. The anti-oxidation activity of the synthesized poly(catechin) was confirmed by xanthine oxidase assay. The elucidation of a uniquely catalytic mechanism in CWPO-C may improve the applicability of the peroxidase/H2O2 catalyst to green polymer chemistry.
DOI: 10.1007/s12010-013-0534-2
PubMed: 24122664
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<author><name sortKey="Pham, L T Mai" sort="Pham, L T Mai" uniqKey="Pham L" first="L T Mai" last="Pham">L T Mai Pham</name>
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<author><name sortKey="Kim, S Jin" sort="Kim, S Jin" uniqKey="Kim S" first="S Jin" last="Kim">S Jin Kim</name>
</author>
<author><name sortKey="Ahn, U Suk" sort="Ahn, U Suk" uniqKey="Ahn U" first="U Suk" last="Ahn">U Suk Ahn</name>
</author>
<author><name sortKey="Choi, J Weon" sort="Choi, J Weon" uniqKey="Choi J" first="J Weon" last="Choi">J Weon Choi</name>
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<author><name sortKey="Song, B Keun" sort="Song, B Keun" uniqKey="Song B" first="B Keun" last="Song">B Keun Song</name>
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<author><name sortKey="Kim, Y Hwan" sort="Kim, Y Hwan" uniqKey="Kim Y" first="Y Hwan" last="Kim">Y Hwan Kim</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antioxidants (metabolism)</term>
<term>Biocatalysis (MeSH)</term>
<term>Catalytic Domain (MeSH)</term>
<term>Catechin (chemistry)</term>
<term>Catechin (metabolism)</term>
<term>Cations (MeSH)</term>
<term>Cell Wall (enzymology)</term>
<term>Chromatography, Gel (MeSH)</term>
<term>Dimerization (MeSH)</term>
<term>Enzyme Stability (MeSH)</term>
<term>Free Radicals (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Molecular Docking Simulation (MeSH)</term>
<term>Mutation (genetics)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peroxidase (metabolism)</term>
<term>Phenols (chemistry)</term>
<term>Phenols (metabolism)</term>
<term>Polymerization (MeSH)</term>
<term>Polyphenols (metabolism)</term>
<term>Populus (enzymology)</term>
<term>Spectrophotometry (MeSH)</term>
<term>Structural Homology, Protein (MeSH)</term>
<term>Thermodynamics (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Antioxydants (métabolisme)</term>
<term>Biocatalyse (MeSH)</term>
<term>Cations (MeSH)</term>
<term>Catéchine (composition chimique)</term>
<term>Catéchine (métabolisme)</term>
<term>Chromatographie sur gel (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Dimérisation (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Mutation (génétique)</term>
<term>Myeloperoxidase (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Paroi cellulaire (enzymologie)</term>
<term>Phénols (composition chimique)</term>
<term>Phénols (métabolisme)</term>
<term>Polymérisation (MeSH)</term>
<term>Polyphénols (métabolisme)</term>
<term>Populus (enzymologie)</term>
<term>Radicaux libres (métabolisme)</term>
<term>Similitude structurale de protéines (MeSH)</term>
<term>Simulation de docking moléculaire (MeSH)</term>
<term>Spectrophotométrie (MeSH)</term>
<term>Stabilité enzymatique (MeSH)</term>
<term>Thermodynamique (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Catechin</term>
<term>Phenols</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antioxidants</term>
<term>Catechin</term>
<term>Free Radicals</term>
<term>Peroxidase</term>
<term>Phenols</term>
<term>Polyphenols</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Catéchine</term>
<term>Phénols</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Paroi cellulaire</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cell Wall</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mutation</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antioxydants</term>
<term>Catéchine</term>
<term>Myeloperoxidase</term>
<term>Phénols</term>
<term>Polyphénols</term>
<term>Radicaux libres</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Biocatalysis</term>
<term>Catalytic Domain</term>
<term>Cations</term>
<term>Chromatography, Gel</term>
<term>Dimerization</term>
<term>Enzyme Stability</term>
<term>Kinetics</term>
<term>Molecular Docking Simulation</term>
<term>Oxidation-Reduction</term>
<term>Polymerization</term>
<term>Spectrophotometry</term>
<term>Structural Homology, Protein</term>
<term>Thermodynamics</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Biocatalyse</term>
<term>Cations</term>
<term>Chromatographie sur gel</term>
<term>Cinétique</term>
<term>Dimérisation</term>
<term>Domaine catalytique</term>
<term>Oxydoréduction</term>
<term>Polymérisation</term>
<term>Similitude structurale de protéines</term>
<term>Simulation de docking moléculaire</term>
<term>Spectrophotométrie</term>
<term>Stabilité enzymatique</term>
<term>Thermodynamique</term>
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<front><div type="abstract" xml:lang="en">Expressed as insoluble forms in Escherichia coli, native cationic cell wall peroxidase (CWPO-C) from the poplar tree and mutant variants were successfully reactivated via refolding experiments and used to elucidate the previously presumed existence of an electron transfer (ET) pathway in the CWPO-C structure. Their catalytic properties were fully characterized through various analyses including steady-state kinetic, direct oxidation of lignin macromolecules and their respective stabilities during the polymerization reactions. The analysis results proved that the 74th residue on the CWPO-C surface plays an important role in catalyzing the macromolecules via supposed ET mechanism. By comparing the residual activities of wild-type CWPO-C and mutant 74W CWPO-C after 3 min, mutation of tyrosine 74 residue to tryptophan increased the radical resistance of peroxidase up to ten times dramatically while maintaining its capability to oxidize lignin macromolecules. Furthermore, extension of poly(catechin) as well as lignin macromolecules with CWPO-C Y74W mutant clearly showed that this radical-resistant peroxidase mutant can increase the molecular weight of various kinds of polyphenolics by using surface-located active site. The anti-oxidation activity of the synthesized poly(catechin) was confirmed by xanthine oxidase assay. The elucidation of a uniquely catalytic mechanism in CWPO-C may improve the applicability of the peroxidase/H2O2 catalyst to green polymer chemistry.</div>
</front>
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<ArticleTitle>Extension of polyphenolics by CWPO-C peroxidase mutant containing radical-robust surface active site.</ArticleTitle>
<Pagination><MedlinePgn>792-805</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Expressed as insoluble forms in Escherichia coli, native cationic cell wall peroxidase (CWPO-C) from the poplar tree and mutant variants were successfully reactivated via refolding experiments and used to elucidate the previously presumed existence of an electron transfer (ET) pathway in the CWPO-C structure. Their catalytic properties were fully characterized through various analyses including steady-state kinetic, direct oxidation of lignin macromolecules and their respective stabilities during the polymerization reactions. The analysis results proved that the 74th residue on the CWPO-C surface plays an important role in catalyzing the macromolecules via supposed ET mechanism. By comparing the residual activities of wild-type CWPO-C and mutant 74W CWPO-C after 3 min, mutation of tyrosine 74 residue to tryptophan increased the radical resistance of peroxidase up to ten times dramatically while maintaining its capability to oxidize lignin macromolecules. Furthermore, extension of poly(catechin) as well as lignin macromolecules with CWPO-C Y74W mutant clearly showed that this radical-resistant peroxidase mutant can increase the molecular weight of various kinds of polyphenolics by using surface-located active site. The anti-oxidation activity of the synthesized poly(catechin) was confirmed by xanthine oxidase assay. The elucidation of a uniquely catalytic mechanism in CWPO-C may improve the applicability of the peroxidase/H2O2 catalyst to green polymer chemistry.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pham</LastName>
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<Initials>LT</Initials>
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