Active site mutagenesis and phospholipid hydroperoxide reductase activity of poplar type II peroxiredoxin.
Identifieur interne : 004323 ( Main/Exploration ); précédent : 004322; suivant : 004324Active site mutagenesis and phospholipid hydroperoxide reductase activity of poplar type II peroxiredoxin.
Auteurs : Nicolas Rouhier [France] ; Eric Gelhaye ; Catherine Corbier ; Jean Pierre JacquotSource :
- Physiologia plantarum [ 1399-3054 ] ; 2004.
Abstract
The nature of the active site and the substrate specificity of poplar type II peroxiredoxin, an enzyme which preferentially uses glutaredoxin as an electron donor, were investigated in this study. The type II peroxiredoxin is able to use phospholipid hydroperoxide nearly as efficiently as hydrogen peroxide. Two of the hyper-conserved amino acid residues in peroxiredoxins have been altered, by site-directed mutagenesis, generating the mutants T48V and R129Q. The two mutant proteins are inactive with hydrogen peroxide or tertiary butyl hydroperoxide as substrates. On the other hand, the mutant enzymes catalyse the degradation of cumene hydroperoxide with low efficiency. This suggests that the thiol-dependent regeneration process of the catalytic cysteine is not affected by the mutations and that all substrates are not accommodated identically in the active site.
DOI: 10.1111/j.0031-9317.2004.0203.x
PubMed: 15032877
Affiliations:
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Université Henri Poincaré, Faculté des Sciences BP 239, 54506 Vandoeuvre Cedex France LCM3B, Groupe Biocristallographie, UMR 7036, UHP, Faculté des Sciences, 54506 Vandoeuvre Cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>UMR 1136 Interaction Arbres Microorganismes INRA-UHP. Université Henri Poincaré, Faculté des Sciences BP 239, 54506 Vandoeuvre Cedex France LCM3B, Groupe Biocristallographie, UMR 7036, UHP, Faculté des Sciences, 54506 Vandoeuvre Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Vandoeuvre</settlement></placeName><orgName type="university">Université Henri Poincaré</orgName></affiliation></author><author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name></author><author><name sortKey="Corbier, Catherine" sort="Corbier, Catherine" uniqKey="Corbier C" first="Catherine" last="Corbier">Catherine Corbier</name></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean Pierre" last="Jacquot">Jean Pierre Jacquot</name></author></analytic><series><title level="j">Physiologia plantarum</title><idno type="eISSN">1399-3054</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The nature of the active site and the substrate specificity of poplar type II peroxiredoxin, an enzyme which preferentially uses glutaredoxin as an electron donor, were investigated in this study. The type II peroxiredoxin is able to use phospholipid hydroperoxide nearly as efficiently as hydrogen peroxide. Two of the hyper-conserved amino acid residues in peroxiredoxins have been altered, by site-directed mutagenesis, generating the mutants T48V and R129Q. The two mutant proteins are inactive with hydrogen peroxide or tertiary butyl hydroperoxide as substrates. On the other hand, the mutant enzymes catalyse the degradation of cumene hydroperoxide with low efficiency. This suggests that the thiol-dependent regeneration process of the catalytic cysteine is not affected by the mutations and that all substrates are not accommodated identically in the active site.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">15032877</PMID><DateRevised><Year>2019</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1399-3054</ISSN><JournalIssue CitedMedium="Internet"><Volume>120</Volume><Issue>1</Issue><PubDate><Year>2004</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Physiologia plantarum</Title><ISOAbbreviation>Physiol Plant</ISOAbbreviation></Journal><ArticleTitle>Active site mutagenesis and phospholipid hydroperoxide reductase activity of poplar type II peroxiredoxin.</ArticleTitle><Pagination><MedlinePgn>57-62</MedlinePgn></Pagination><Abstract><AbstractText>The nature of the active site and the substrate specificity of poplar type II peroxiredoxin, an enzyme which preferentially uses glutaredoxin as an electron donor, were investigated in this study. The type II peroxiredoxin is able to use phospholipid hydroperoxide nearly as efficiently as hydrogen peroxide. Two of the hyper-conserved amino acid residues in peroxiredoxins have been altered, by site-directed mutagenesis, generating the mutants T48V and R129Q. The two mutant proteins are inactive with hydrogen peroxide or tertiary butyl hydroperoxide as substrates. On the other hand, the mutant enzymes catalyse the degradation of cumene hydroperoxide with low efficiency. This suggests that the thiol-dependent regeneration process of the catalytic cysteine is not affected by the mutations and that all substrates are not accommodated identically in the active site.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>UMR 1136 Interaction Arbres Microorganismes INRA-UHP. Université Henri Poincaré, Faculté des Sciences BP 239, 54506 Vandoeuvre Cedex France LCM3B, Groupe Biocristallographie, UMR 7036, UHP, Faculté des Sciences, 54506 Vandoeuvre Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Corbier</LastName><ForeName>Catherine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean Pierre</ForeName><Initials>JP</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Denmark</Country><MedlineTA>Physiol Plant</MedlineTA><NlmUniqueID>1256322</NlmUniqueID><ISSNLinking>0031-9317</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>3</Month><Day>23</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>3</Month><Day>23</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>3</Month><Day>23</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15032877</ArticleId><ArticleId IdType="doi">10.1111/j.0031-9317.2004.0203.x</ArticleId><ArticleId IdType="pii">PPL203</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Vandoeuvre</li></settlement><orgName><li>Université Henri Poincaré</li></orgName></list><tree><noCountry><name sortKey="Corbier, Catherine" sort="Corbier, Catherine" uniqKey="Corbier C" first="Catherine" last="Corbier">Catherine Corbier</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean Pierre" last="Jacquot">Jean Pierre Jacquot</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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