The effects of calcium on the thermal stability and activity of manganese peroxidase.
Identifieur interne : 000C28 ( Main/Exploration ); précédent : 000C27; suivant : 000C29The effects of calcium on the thermal stability and activity of manganese peroxidase.
Auteurs : G R Sutherland [États-Unis] ; S D AustSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1996.
Descripteurs français
- KwdFr :
- Basidiomycota (enzymologie), Calcium (pharmacologie), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Conformation des protéines (effets des médicaments et des substances chimiques), Dénaturation des protéines (effets des médicaments et des substances chimiques), Hème (composition chimique), Peroxidases (antagonistes et inhibiteurs), Peroxidases (composition chimique), Peroxidases (métabolisme), Stabilité enzymatique (effets des médicaments et des substances chimiques), Température (MeSH).
- MESH :
- antagonistes et inhibiteurs : Peroxidases.
- composition chimique : Hème, Peroxidases.
- effets des médicaments et des substances chimiques : Conformation des protéines, Dénaturation des protéines, Stabilité enzymatique.
- enzymologie : Basidiomycota.
- métabolisme : Peroxidases.
- pharmacologie : Calcium.
- Cinétique, Concentration en ions d'hydrogène, Température.
English descriptors
- KwdEn :
- Basidiomycota (enzymology), Calcium (pharmacology), Enzyme Stability (drug effects), Heme (chemistry), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), Peroxidases (antagonists & inhibitors), Peroxidases (chemistry), Peroxidases (metabolism), Protein Conformation (drug effects), Protein Denaturation (drug effects), Temperature (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Peroxidases.
- chemical , chemistry : Heme, Peroxidases.
- chemical , metabolism : Peroxidases.
- chemical , pharmacology : Calcium.
- drug effects : Enzyme Stability, Protein Conformation, Protein Denaturation.
- enzymology : Basidiomycota.
- Hydrogen-Ion Concentration, Kinetics, Temperature.
Abstract
The presence of micromolar Ca2+ efficiently prevented the thermal inactivation of manganese peroxidase from Phanerochaete chrysosporium. The amount of Ca2+ normally present in the enzyme decreased when the enzyme was thermally inactivated and EGTA increased the rate of inactivation. The inactivation kinetics were biphasic, suggesting a sequential two-step process. The rate of inactivation during the second, slower step corresponded to the rate of loss of heme from the enzyme. Thermally inactivated manganese peroxidase could be readily reactivated in the presence of excess Ca2+. However, as the time of thermal incubation increased and the amount of remaining heme decreased, the amount of enzyme activity recovered decreased. Therefore, while both steps of denaturation could be prevented by Ca2+, only one step could be reversed upon the addition of Ca2+. It is proposed that the first step of denaturation involves the loss of Ca2+ which causes conformational changes resulting in the loss of manganese peroxidase activity. The second step is believed to involve further structural loss and results in the loss of heme from the enzyme. It is concluded that manganese peroxidase is susceptible to thermal inactivation because it contains relatively labile Ca2+ ions required for stability and activity.
DOI: 10.1006/abbi.1996.0324
PubMed: 8806717
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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The amount of Ca2+ normally present in the enzyme decreased when the enzyme was thermally inactivated and EGTA increased the rate of inactivation. The inactivation kinetics were biphasic, suggesting a sequential two-step process. The rate of inactivation during the second, slower step corresponded to the rate of loss of heme from the enzyme. Thermally inactivated manganese peroxidase could be readily reactivated in the presence of excess Ca2+. However, as the time of thermal incubation increased and the amount of remaining heme decreased, the amount of enzyme activity recovered decreased. Therefore, while both steps of denaturation could be prevented by Ca2+, only one step could be reversed upon the addition of Ca2+. It is proposed that the first step of denaturation involves the loss of Ca2+ which causes conformational changes resulting in the loss of manganese peroxidase activity. The second step is believed to involve further structural loss and results in the loss of heme from the enzyme. It is concluded that manganese peroxidase is susceptible to thermal inactivation because it contains relatively labile Ca2+ ions required for stability and activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8806717</PMID><DateCompleted><Year>1996</Year><Month>10</Month><Day>24</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>332</Volume><Issue>1</Issue><PubDate><Year>1996</Year><Month>Aug</Month><Day>01</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>The effects of calcium on the thermal stability and activity of manganese peroxidase.</ArticleTitle><Pagination><MedlinePgn>128-34</MedlinePgn></Pagination><Abstract><AbstractText>The presence of micromolar Ca2+ efficiently prevented the thermal inactivation of manganese peroxidase from Phanerochaete chrysosporium. The amount of Ca2+ normally present in the enzyme decreased when the enzyme was thermally inactivated and EGTA increased the rate of inactivation. The inactivation kinetics were biphasic, suggesting a sequential two-step process. The rate of inactivation during the second, slower step corresponded to the rate of loss of heme from the enzyme. Thermally inactivated manganese peroxidase could be readily reactivated in the presence of excess Ca2+. However, as the time of thermal incubation increased and the amount of remaining heme decreased, the amount of enzyme activity recovered decreased. Therefore, while both steps of denaturation could be prevented by Ca2+, only one step could be reversed upon the addition of Ca2+. It is proposed that the first step of denaturation involves the loss of Ca2+ which causes conformational changes resulting in the loss of manganese peroxidase activity. The second step is believed to involve further structural loss and results in the loss of heme from the enzyme. It is concluded that manganese peroxidase is susceptible to thermal inactivation because it contains relatively labile Ca2+ ions required for stability and activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sutherland</LastName><ForeName>G R</ForeName><Initials>GR</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><GrantList CompleteYN="Y"><Grant><GrantID>ES04922</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber><NameOfSubstance UI="D002118">Calcium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year><Month>8</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1996</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1996</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8806717</ArticleId><ArticleId IdType="pii">S0003-9861(96)90324-0</ArticleId><ArticleId IdType="doi">10.1006/abbi.1996.0324</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="Sutherland, G R" sort="Sutherland, G R" uniqKey="Sutherland G" first="G R" last="Sutherland">G R Sutherland</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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