Effects of Mn2+ and oxalate on the catalatic activity of manganese peroxidase.
Identifieur interne : 000B97 ( Main/Corpus ); précédent : 000B96; suivant : 000B98Effects of Mn2+ and oxalate on the catalatic activity of manganese peroxidase.
Auteurs : S L Timofeevski ; S D AustSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1997.
English descriptors
- KwdEn :
- Animals (MeSH), Basidiomycota (enzymology), Catalase (antagonists & inhibitors), Catalase (drug effects), Catalase (metabolism), Cattle (MeSH), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), Manganese (metabolism), Manganese (pharmacology), Oxalates (metabolism), Oxalates (pharmacology), Oxygen (metabolism), Peroxidases (drug effects), Peroxidases (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Catalase.
- chemical , drug effects : Catalase, Peroxidases.
- enzymology : Basidiomycota.
- chemical , metabolism : Catalase, Manganese, Oxalates, Oxygen, Peroxidases.
- chemical , pharmacology : Manganese, Oxalates.
- Animals, Cattle, Hydrogen-Ion Concentration, Kinetics.
Abstract
Manganese peroxidase from Phanerochaete chrysosporium is an extracellular heme-containing enzyme known to catalyze the oxidation of Mn2+ to Mn3+ in a reaction requiring oxalate or another appropriate manganese chelator. We have found that the enzyme can also catalyze a manganese-dependent disproportionation of hydrogen peroxide when a manganese chelator is not included. The catalatic activity was observed in the pH range from 3.0 to 8.5, and the apparent second-order rate constant for catalatic reaction was about 2 x 10(5) M-1 s-1 at pH 4.5 to 7.0 at 25 degrees C. Oxalate inhibited oxygen production by increasing the apparent K(m) for Mn2+ for catalatic activity from micromolar to millimolar levels and facilitating peroxidase activity. Catalase-type function was recovered by excess of Mn2+ in the presence of oxalate. We propose that catalatic activity may protect the enzyme from inactivation by hydrogen peroxide in an environment where free oxalate may be limited.
DOI: 10.1006/bbrc.1997.7453
PubMed: 9367821
Links to Exploration step
pubmed:9367821Le document en format XML
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<author><name sortKey="Timofeevski, S L" sort="Timofeevski, S L" uniqKey="Timofeevski S" first="S L" last="Timofeevski">S L Timofeevski</name>
<affiliation><nlm:affiliation>Biotechnology Center, Utah State University, Logan 84322-4705, USA.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Effects of Mn2+ and oxalate on the catalatic activity of manganese peroxidase.</title>
<author><name sortKey="Timofeevski, S L" sort="Timofeevski, S L" uniqKey="Timofeevski S" first="S L" last="Timofeevski">S L Timofeevski</name>
<affiliation><nlm:affiliation>Biotechnology Center, Utah State University, Logan 84322-4705, USA.</nlm:affiliation>
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<author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name>
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<series><title level="j">Biochemical and biophysical research communications</title>
<idno type="ISSN">0006-291X</idno>
<imprint><date when="1997" type="published">1997</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term>
<term>Basidiomycota (enzymology)</term>
<term>Catalase (antagonists & inhibitors)</term>
<term>Catalase (drug effects)</term>
<term>Catalase (metabolism)</term>
<term>Cattle (MeSH)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Manganese (metabolism)</term>
<term>Manganese (pharmacology)</term>
<term>Oxalates (metabolism)</term>
<term>Oxalates (pharmacology)</term>
<term>Oxygen (metabolism)</term>
<term>Peroxidases (drug effects)</term>
<term>Peroxidases (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Catalase</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Catalase</term>
<term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Catalase</term>
<term>Manganese</term>
<term>Oxalates</term>
<term>Oxygen</term>
<term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Manganese</term>
<term>Oxalates</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cattle</term>
<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
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<front><div type="abstract" xml:lang="en">Manganese peroxidase from Phanerochaete chrysosporium is an extracellular heme-containing enzyme known to catalyze the oxidation of Mn2+ to Mn3+ in a reaction requiring oxalate or another appropriate manganese chelator. We have found that the enzyme can also catalyze a manganese-dependent disproportionation of hydrogen peroxide when a manganese chelator is not included. The catalatic activity was observed in the pH range from 3.0 to 8.5, and the apparent second-order rate constant for catalatic reaction was about 2 x 10(5) M-1 s-1 at pH 4.5 to 7.0 at 25 degrees C. Oxalate inhibited oxygen production by increasing the apparent K(m) for Mn2+ for catalatic activity from micromolar to millimolar levels and facilitating peroxidase activity. Catalase-type function was recovered by excess of Mn2+ in the presence of oxalate. We propose that catalatic activity may protect the enzyme from inactivation by hydrogen peroxide in an environment where free oxalate may be limited.</div>
</front>
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<DateCompleted><Year>1997</Year>
<Month>12</Month>
<Day>12</Day>
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<DateRevised><Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
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<Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN>
<JournalIssue CitedMedium="Print"><Volume>239</Volume>
<Issue>3</Issue>
<PubDate><Year>1997</Year>
<Month>Oct</Month>
<Day>29</Day>
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<Title>Biochemical and biophysical research communications</Title>
<ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation>
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<ArticleTitle>Effects of Mn2+ and oxalate on the catalatic activity of manganese peroxidase.</ArticleTitle>
<Pagination><MedlinePgn>645-9</MedlinePgn>
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<Abstract><AbstractText>Manganese peroxidase from Phanerochaete chrysosporium is an extracellular heme-containing enzyme known to catalyze the oxidation of Mn2+ to Mn3+ in a reaction requiring oxalate or another appropriate manganese chelator. We have found that the enzyme can also catalyze a manganese-dependent disproportionation of hydrogen peroxide when a manganese chelator is not included. The catalatic activity was observed in the pH range from 3.0 to 8.5, and the apparent second-order rate constant for catalatic reaction was about 2 x 10(5) M-1 s-1 at pH 4.5 to 7.0 at 25 degrees C. Oxalate inhibited oxygen production by increasing the apparent K(m) for Mn2+ for catalatic activity from micromolar to millimolar levels and facilitating peroxidase activity. Catalase-type function was recovered by excess of Mn2+ in the presence of oxalate. We propose that catalatic activity may protect the enzyme from inactivation by hydrogen peroxide in an environment where free oxalate may be limited.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Timofeevski</LastName>
<ForeName>S L</ForeName>
<Initials>SL</Initials>
<AffiliationInfo><Affiliation>Biotechnology Center, Utah State University, Logan 84322-4705, USA.</Affiliation>
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<ForeName>S D</ForeName>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010070">Oxalates</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber>
<NameOfSubstance UI="D008345">Manganese</NameOfSubstance>
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<Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber>
<NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance>
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<Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber>
<NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance>
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<Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber>
<NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.11.1.6</RegistryNumber>
<NameOfSubstance UI="D002374">Catalase</NameOfSubstance>
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<Chemical><RegistryNumber>S88TT14065</RegistryNumber>
<NameOfSubstance UI="D010100">Oxygen</NameOfSubstance>
</Chemical>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
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<MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002374" MajorTopicYN="N">Catalase</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName>
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<MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName>
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<MeshHeading><DescriptorName UI="D008345" MajorTopicYN="N">Manganese</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010070" MajorTopicYN="N">Oxalates</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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