Engineering of the H2O2-binding pocket region of a recombinant manganese peroxidase to be resistant to H2O2.
Identifieur interne : 000A28 ( Main/Corpus ); précédent : 000A27; suivant : 000A29Engineering of the H2O2-binding pocket region of a recombinant manganese peroxidase to be resistant to H2O2.
Auteurs : C. Miyazaki ; H. TakahashiSource :
- FEBS letters [ 0014-5793 ] ; 2001.
English descriptors
- KwdEn :
- Binding Sites (MeSH), Dose-Response Relationship, Drug (MeSH), Escherichia coli (metabolism), Hydrogen Peroxide (metabolism), Methionine (chemistry), Models, Molecular (MeSH), Mutagenesis, Site-Directed (MeSH), Mutation (MeSH), Oxygen (metabolism), Peroxidases (chemistry), Peroxidases (metabolism), Phanerochaete (enzymology), Protein Binding (MeSH), Protein Conformation (MeSH), Protein Folding (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism).
- MESH :
- chemical , chemistry : Methionine, Peroxidases, Recombinant Proteins.
- chemical , metabolism : Hydrogen Peroxide, Oxygen, Peroxidases, Recombinant Proteins.
- enzymology : Phanerochaete.
- metabolism : Escherichia coli.
- Binding Sites, Dose-Response Relationship, Drug, Models, Molecular, Mutagenesis, Site-Directed, Mutation, Protein Binding, Protein Conformation, Protein Folding.
Abstract
The manganese peroxidase produced by Phanerochaete chrysosporium, which catalyzes the oxidation of Mn(2+) to Mn(3+), is easily inactivated by the hydrogen peroxide (H2O2) presented in the reaction. We attempted to increase H2O2 resistance by the conformational stabilization around the H2O2-binding pocket. Based on its structural model, engineering of oxidizable Met273 located near the pocket to a non-oxidizable Leu showed a great improvement. Furthermore, after treatment at 1 mM H2O2 where the wild-type is completely inactivated, full activity can be retained by engineering the Asn81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser.
DOI: 10.1016/s0014-5793(01)03127-1
PubMed: 11734216
Links to Exploration step
pubmed:11734216Le document en format XML
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<author><name sortKey="Miyazaki, C" sort="Miyazaki, C" uniqKey="Miyazaki C" first="C" last="Miyazaki">C. Miyazaki</name>
<affiliation><nlm:affiliation>Toyota Central R&D Labs., 41-1, Yokomichi, Aichi 480-1192, Nagakute, Japan.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Takahashi, H" sort="Takahashi, H" uniqKey="Takahashi H" first="H" last="Takahashi">H. Takahashi</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term>
<term>Dose-Response Relationship, Drug (MeSH)</term>
<term>Escherichia coli (metabolism)</term>
<term>Hydrogen Peroxide (metabolism)</term>
<term>Methionine (chemistry)</term>
<term>Models, Molecular (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Oxygen (metabolism)</term>
<term>Peroxidases (chemistry)</term>
<term>Peroxidases (metabolism)</term>
<term>Phanerochaete (enzymology)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Conformation (MeSH)</term>
<term>Protein Folding (MeSH)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (metabolism)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Methionine</term>
<term>Peroxidases</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hydrogen Peroxide</term>
<term>Oxygen</term>
<term>Peroxidases</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term>
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<term>Dose-Response Relationship, Drug</term>
<term>Models, Molecular</term>
<term>Mutagenesis, Site-Directed</term>
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<front><div type="abstract" xml:lang="en">The manganese peroxidase produced by Phanerochaete chrysosporium, which catalyzes the oxidation of Mn(2+) to Mn(3+), is easily inactivated by the hydrogen peroxide (H2O2) presented in the reaction. We attempted to increase H2O2 resistance by the conformational stabilization around the H2O2-binding pocket. Based on its structural model, engineering of oxidizable Met273 located near the pocket to a non-oxidizable Leu showed a great improvement. Furthermore, after treatment at 1 mM H2O2 where the wild-type is completely inactivated, full activity can be retained by engineering the Asn81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser.</div>
</front>
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<DateRevised><Year>2019</Year>
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<Title>FEBS letters</Title>
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<Abstract><AbstractText>The manganese peroxidase produced by Phanerochaete chrysosporium, which catalyzes the oxidation of Mn(2+) to Mn(3+), is easily inactivated by the hydrogen peroxide (H2O2) presented in the reaction. We attempted to increase H2O2 resistance by the conformational stabilization around the H2O2-binding pocket. Based on its structural model, engineering of oxidizable Met273 located near the pocket to a non-oxidizable Leu showed a great improvement. Furthermore, after treatment at 1 mM H2O2 where the wild-type is completely inactivated, full activity can be retained by engineering the Asn81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser.</AbstractText>
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