Plant peroxiredoxins: catalytic mechanisms, functional significance and future perspectives.
Identifieur interne : 000895 ( Main/Exploration ); précédent : 000894; suivant : 000896Plant peroxiredoxins: catalytic mechanisms, functional significance and future perspectives.
Auteurs : Indu Bhatt [Inde] ; B N TripathiSource :
- Biotechnology advances [ 1873-1899 ]
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Peroxirédoxines, Protéines végétales.
- métabolisme : Peroxirédoxines, Protéines végétales.
- Oxydoréduction, Photosynthèse, Stress oxydatif, Transduction du signal.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Peroxiredoxins, Plant Proteins.
- chemical , metabolism : Peroxiredoxins, Plant Proteins.
- Oxidation-Reduction, Oxidative Stress, Photosynthesis, Signal Transduction.
Abstract
Peroxiredoxins (Prx) are a family of thiol dependent peroxidases found in almost all kingdoms. In plants, five major classes of Prx are known. They are known to catalyze the decomposition of peroxides and as they lack a prosthetic group, the catalytic cycle results in the generation of an inactive form of Prx. In order to regain the active form, Prx rely on external electron donors such as thioredoxins, glutaredoxins, cyclophilins, NADPH-dependent thioredoxin reductase C (NTRC) etc. In addition to their well established role in antioxidative defense, Prx are also reported to play an important role in growth and development, dessication tolerance in dormant seeds, protection of photosynthesis, defense against pathogens and redox signaling. Prx are also known to establish an alternate water-water cycle for the detoxification of H₂O₂, parallel to ascorbate-dependent H₂O₂ detoxification. But the relative contribution of Prx in detoxifying H₂O₂ compared to ascorbate peroxidase is not known so far due to experimental limitations. In view of the above, the present review focuses on the recent developments on Prxs.
DOI: 10.1016/j.biotechadv.2011.07.002
PubMed: 21777667
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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In plants, five major classes of Prx are known. They are known to catalyze the decomposition of peroxides and as they lack a prosthetic group, the catalytic cycle results in the generation of an inactive form of Prx. In order to regain the active form, Prx rely on external electron donors such as thioredoxins, glutaredoxins, cyclophilins, NADPH-dependent thioredoxin reductase C (NTRC) etc. In addition to their well established role in antioxidative defense, Prx are also reported to play an important role in growth and development, dessication tolerance in dormant seeds, protection of photosynthesis, defense against pathogens and redox signaling. Prx are also known to establish an alternate water-water cycle for the detoxification of H₂O₂, parallel to ascorbate-dependent H₂O₂ detoxification. But the relative contribution of Prx in detoxifying H₂O₂ compared to ascorbate peroxidase is not known so far due to experimental limitations. In view of the above, the present review focuses on the recent developments on Prxs.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21777667</PMID><DateCompleted><Year>2012</Year><Month>01</Month><Day>19</Day></DateCompleted><DateRevised><Year>2011</Year><Month>10</Month><Day>04</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-1899</ISSN><JournalIssue CitedMedium="Internet"><Volume>29</Volume><Issue>6</Issue><PubDate><MedlineDate>2011 Nov-Dec</MedlineDate></PubDate></JournalIssue><Title>Biotechnology advances</Title><ISOAbbreviation>Biotechnol Adv</ISOAbbreviation></Journal><ArticleTitle>Plant peroxiredoxins: catalytic mechanisms, functional significance and future perspectives.</ArticleTitle><Pagination><MedlinePgn>850-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.biotechadv.2011.07.002</ELocationID><Abstract><AbstractText>Peroxiredoxins (Prx) are a family of thiol dependent peroxidases found in almost all kingdoms. In plants, five major classes of Prx are known. They are known to catalyze the decomposition of peroxides and as they lack a prosthetic group, the catalytic cycle results in the generation of an inactive form of Prx. In order to regain the active form, Prx rely on external electron donors such as thioredoxins, glutaredoxins, cyclophilins, NADPH-dependent thioredoxin reductase C (NTRC) etc. In addition to their well established role in antioxidative defense, Prx are also reported to play an important role in growth and development, dessication tolerance in dormant seeds, protection of photosynthesis, defense against pathogens and redox signaling. Prx are also known to establish an alternate water-water cycle for the detoxification of H₂O₂, parallel to ascorbate-dependent H₂O₂ detoxification. But the relative contribution of Prx in detoxifying H₂O₂ compared to ascorbate peroxidase is not known so far due to experimental limitations. In view of the above, the present review focuses on the recent developments on Prxs.</AbstractText><CopyrightInformation>Copyright © 2011 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bhatt</LastName><ForeName>Indu</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Department of Bioscience and Biotechnology, Banasthali University, Banasthali 304022, Rajasthan, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tripathi</LastName><ForeName>B N</ForeName><Initials>BN</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>07</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biotechnol Adv</MedlineTA><NlmUniqueID>8403708</NlmUniqueID><ISSNLinking>0734-9750</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010788" MajorTopicYN="N">Photosynthesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>02</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2011</Year><Month>06</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>07</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>7</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>7</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>1</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21777667</ArticleId><ArticleId IdType="pii">S0734-9750(11)00099-1</ArticleId><ArticleId IdType="doi">10.1016/j.biotechadv.2011.07.002</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Inde</li></country></list><tree><noCountry><name sortKey="Tripathi, B N" sort="Tripathi, B N" uniqKey="Tripathi B" first="B N" last="Tripathi">B N Tripathi</name></noCountry><country name="Inde"><noRegion><name sortKey="Bhatt, Indu" sort="Bhatt, Indu" uniqKey="Bhatt I" first="Indu" last="Bhatt">Indu Bhatt</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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