Effects of Mn2+ and oxalate on the catalatic activity of manganese peroxidase.
Identifieur interne : 000C14 ( Main/Exploration ); précédent : 000C13; suivant : 000C15Effects of Mn2+ and oxalate on the catalatic activity of manganese peroxidase.
Auteurs : S L Timofeevski [États-Unis] ; S D AustSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1997.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Basidiomycota (enzymologie), Bovins (MeSH), Catalase (antagonistes et inhibiteurs), Catalase (effets des médicaments et des substances chimiques), Catalase (métabolisme), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Manganèse (métabolisme), Manganèse (pharmacologie), Oxalates (métabolisme), Oxalates (pharmacologie), Oxygène (métabolisme), Peroxidases (effets des médicaments et des substances chimiques), Peroxidases (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Catalase.
- effets des médicaments et des substances chimiques : Catalase, Peroxidases.
- enzymologie : Basidiomycota.
- métabolisme : Catalase, Manganèse, Oxalates, Oxygène, Peroxidases.
- pharmacologie : Manganèse, Oxalates.
- Animaux, Bovins, Cinétique, Concentration en ions d'hydrogène.
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
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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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></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Cinétique</term><term>Concentration en ions d'hydrogène</term></keywords></textClass></profileDesc></teiHeader><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></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9367821</PMID><DateCompleted><Year>1997</Year><Month>12</Month><Day>12</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><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></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Effects of Mn2+ and oxalate on the catalatic activity of manganese peroxidase.</ArticleTitle><Pagination><MedlinePgn>645-9</MedlinePgn></Pagination><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></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aust</LastName><ForeName>S D</ForeName><Initials>SD</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010070">Oxalates</NameOfSubstance></Chemical><Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber><NameOfSubstance UI="D008345">Manganese</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><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></Chemical><Chemical><RegistryNumber>S88TT14065</RegistryNumber><NameOfSubstance UI="D010100">Oxygen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><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></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><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></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>11</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>11</Month><Day>21</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>11</Month><Day>21</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9367821</ArticleId><ArticleId IdType="pii">S0006-291X(97)97453-2</ArticleId><ArticleId IdType="doi">10.1006/bbrc.1997.7453</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Timofeevski, S L" sort="Timofeevski, S L" uniqKey="Timofeevski S" first="S L" last="Timofeevski">S L Timofeevski</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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