Plant aldo-keto reductases (AKRs) as multi-tasking soldiers involved in diverse plant metabolic processes and stress defense: A structure-function update.
Identifieur interne : 001B95 ( Main/Exploration ); précédent : 001B94; suivant : 001B96Plant aldo-keto reductases (AKRs) as multi-tasking soldiers involved in diverse plant metabolic processes and stress defense: A structure-function update.
Auteurs : Debashree Sengupta [Inde] ; Dhiraj Naik [Inde] ; Attipalli R. Reddy [Inde]Source :
- Journal of plant physiology [ 1618-1328 ] ; 2015.
Descripteurs français
- KwdFr :
- Aldo-keto reductases (MeSH), Aldose reductase (composition chimique), Aldose reductase (métabolisme), Données de séquences moléculaires (MeSH), Plantes (enzymologie), Plantes (métabolisme), Relation structure-activité (MeSH), Similitude structurale de protéines (MeSH), Stress physiologique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Aldose reductase.
- enzymologie : Plantes.
- métabolisme : Aldose reductase, Plantes.
- Aldo-keto reductases, Données de séquences moléculaires, Relation structure-activité, Similitude structurale de protéines, Stress physiologique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Aldehyde Reductase (chemistry), Aldehyde Reductase (metabolism), Aldo-Keto Reductases (MeSH), Amino Acid Sequence (MeSH), Molecular Sequence Data (MeSH), Plants (enzymology), Plants (metabolism), Stress, Physiological (MeSH), Structural Homology, Protein (MeSH), Structure-Activity Relationship (MeSH).
- MESH :
- chemical , chemistry : Aldehyde Reductase.
- chemical , metabolism : Aldehyde Reductase.
- chemical : Aldo-Keto Reductases.
- enzymology : Plants.
- metabolism : Plants.
- Amino Acid Sequence, Molecular Sequence Data, Stress, Physiological, Structural Homology, Protein, Structure-Activity Relationship.
Abstract
The aldo-keto reductase (AKR) superfamily comprises of a large number of primarily monomeric protein members, which reduce a broad spectrum of substrates ranging from simple sugars to potentially toxic aldehydes. Plant AKRs can be broadly categorized into four important functional groups, which highlight their roles in diverse plant metabolic reactions including reactive aldehyde detoxification, biosynthesis of osmolytes, secondary metabolism and membrane transport. Further, multiple overlapping functional aspects of plant AKRs including biotic and abiotic stress defense, production of commercially important secondary metabolites, iron acquisition from soil, plant-microbe interactions etc. are discussed as subcategories within respective major groups. Owing to the broad substrate specificity and multiple stress tolerance of the well-characterized AKR4C9 from Arabidopsis thaliana, protein sequences of all the homologues of AKR4C9 (A9-like proteins) from forty different plant species (Phytozome database) were analyzed. The analysis revealed that all A9-like proteins possess strictly conserved key catalytic residues (D-47, Y-52 and K-81) and belong to the pfam00248 and cl00470 AKR superfamilies. Based on structural homology of the three flexible loops of AKR4C9 (Loop A, B and C) responsible for broad substrate specificity, A9-like proteins found in Brassica rapa, Phaseolus vulgaris, Cucumis sativus, Populus trichocarpa and Solanum lycopersicum were predicted to have a similar range of substrate specificity. Thus, plant AKRs can be considered as potential breeding targets for developing stress tolerant varieties in the future. The present review provides a consolidated update on the current research status of plant AKRs with an emphasis on important functional aspects as well as their potential future prospects and an insight into the overall structure-function relationships of A9-like proteins.
DOI: 10.1016/j.jplph.2015.03.004
PubMed: 25840343
Affiliations:
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Plant AKRs can be broadly categorized into four important functional groups, which highlight their roles in diverse plant metabolic reactions including reactive aldehyde detoxification, biosynthesis of osmolytes, secondary metabolism and membrane transport. Further, multiple overlapping functional aspects of plant AKRs including biotic and abiotic stress defense, production of commercially important secondary metabolites, iron acquisition from soil, plant-microbe interactions etc. are discussed as subcategories within respective major groups. Owing to the broad substrate specificity and multiple stress tolerance of the well-characterized AKR4C9 from Arabidopsis thaliana, protein sequences of all the homologues of AKR4C9 (A9-like proteins) from forty different plant species (Phytozome database) were analyzed. The analysis revealed that all A9-like proteins possess strictly conserved key catalytic residues (D-47, Y-52 and K-81) and belong to the pfam00248 and cl00470 AKR superfamilies. Based on structural homology of the three flexible loops of AKR4C9 (Loop A, B and C) responsible for broad substrate specificity, A9-like proteins found in Brassica rapa, Phaseolus vulgaris, Cucumis sativus, Populus trichocarpa and Solanum lycopersicum were predicted to have a similar range of substrate specificity. Thus, plant AKRs can be considered as potential breeding targets for developing stress tolerant varieties in the future. The present review provides a consolidated update on the current research status of plant AKRs with an emphasis on important functional aspects as well as their potential future prospects and an insight into the overall structure-function relationships of A9-like proteins. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25840343</PMID><DateCompleted><Year>2016</Year><Month>01</Month><Day>26</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1618-1328</ISSN><JournalIssue CitedMedium="Internet"><Volume>179</Volume><PubDate><Year>2015</Year><Month>May</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of plant physiology</Title><ISOAbbreviation>J Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Plant aldo-keto reductases (AKRs) as multi-tasking soldiers involved in diverse plant metabolic processes and stress defense: A structure-function update.</ArticleTitle><Pagination><MedlinePgn>40-55</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jplph.2015.03.004</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0176-1617(15)00057-7</ELocationID><Abstract><AbstractText>The aldo-keto reductase (AKR) superfamily comprises of a large number of primarily monomeric protein members, which reduce a broad spectrum of substrates ranging from simple sugars to potentially toxic aldehydes. Plant AKRs can be broadly categorized into four important functional groups, which highlight their roles in diverse plant metabolic reactions including reactive aldehyde detoxification, biosynthesis of osmolytes, secondary metabolism and membrane transport. Further, multiple overlapping functional aspects of plant AKRs including biotic and abiotic stress defense, production of commercially important secondary metabolites, iron acquisition from soil, plant-microbe interactions etc. are discussed as subcategories within respective major groups. Owing to the broad substrate specificity and multiple stress tolerance of the well-characterized AKR4C9 from Arabidopsis thaliana, protein sequences of all the homologues of AKR4C9 (A9-like proteins) from forty different plant species (Phytozome database) were analyzed. The analysis revealed that all A9-like proteins possess strictly conserved key catalytic residues (D-47, Y-52 and K-81) and belong to the pfam00248 and cl00470 AKR superfamilies. Based on structural homology of the three flexible loops of AKR4C9 (Loop A, B and C) responsible for broad substrate specificity, A9-like proteins found in Brassica rapa, Phaseolus vulgaris, Cucumis sativus, Populus trichocarpa and Solanum lycopersicum were predicted to have a similar range of substrate specificity. Thus, plant AKRs can be considered as potential breeding targets for developing stress tolerant varieties in the future. The present review provides a consolidated update on the current research status of plant AKRs with an emphasis on important functional aspects as well as their potential future prospects and an insight into the overall structure-function relationships of A9-like proteins. </AbstractText><CopyrightInformation>Copyright © 2015. Published by Elsevier GmbH.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sengupta</LastName><ForeName>Debashree</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Environmental Biotechnology and Ecological Sciences, Indian Institute of Advanced Research, Gandhinagar 382007, Gujarat, India; Department of Plant Sciences, School of Life Sciences, University of Hyderabad, Hyderabad 500046, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Naik</LastName><ForeName>Dhiraj</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Environmental Biotechnology and Ecological Sciences, Indian Institute of Advanced Research, Gandhinagar 382007, Gujarat, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Reddy</LastName><ForeName>Attipalli R</ForeName><Initials>AR</Initials><AffiliationInfo><Affiliation>Department of Plant Sciences, School of Life Sciences, University of Hyderabad, Hyderabad 500046, India. Electronic address: arrsl@uohyd.ernet.in.</Affiliation></AffiliationInfo></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>2015</Year><Month>03</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>J Plant Physiol</MedlineTA><NlmUniqueID>9882059</NlmUniqueID><ISSNLinking>0176-1617</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 1.1.1.-</RegistryNumber><NameOfSubstance UI="D000074408">Aldo-Keto Reductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.21</RegistryNumber><NameOfSubstance UI="D000449">Aldehyde Reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000449" MajorTopicYN="N">Aldehyde Reductase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000074408" MajorTopicYN="N">Aldo-Keto Reductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013312" MajorTopicYN="Y">Stress, Physiological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D040681" MajorTopicYN="N">Structural Homology, Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">A9-like protein</Keyword><Keyword MajorTopicYN="N">AKR4C9</Keyword><Keyword MajorTopicYN="N">Plant AKR</Keyword><Keyword MajorTopicYN="N">Reactive aldehyde</Keyword><Keyword MajorTopicYN="N">Stress tolerance</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>11</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>03</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>03</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>1</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25840343</ArticleId><ArticleId IdType="pii">S0176-1617(15)00057-7</ArticleId><ArticleId IdType="doi">10.1016/j.jplph.2015.03.004</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Inde</li></country></list><tree><country name="Inde"><noRegion><name sortKey="Sengupta, Debashree" sort="Sengupta, Debashree" uniqKey="Sengupta D" first="Debashree" last="Sengupta">Debashree Sengupta</name></noRegion><name sortKey="Naik, Dhiraj" sort="Naik, Dhiraj" uniqKey="Naik D" first="Dhiraj" last="Naik">Dhiraj Naik</name><name sortKey="Reddy, Attipalli R" sort="Reddy, Attipalli R" uniqKey="Reddy A" first="Attipalli R" last="Reddy">Attipalli R. 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