Salicyl alcohol oxidase of the chemical defense secretion of two chrysomelid leaf beetles. Molecular and functional characterization of two new members of the glucose-methanol-choline oxidoreductase gene family.
Identifieur interne : 003822 ( Main/Exploration ); précédent : 003821; suivant : 003823Salicyl alcohol oxidase of the chemical defense secretion of two chrysomelid leaf beetles. Molecular and functional characterization of two new members of the glucose-methanol-choline oxidoreductase gene family.
Auteurs : Carmen Michalski [Allemagne] ; Hoda Mohagheghi ; Manfred Nimtz ; Jacques Pasteels ; Dietrich OberSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2008.
Descripteurs français
- KwdFr :
- Alcohol oxidoreductases (génétique), Alcohol oxidoreductases (métabolisme), Alcools benzyliques (métabolisme), Aldéhydes (métabolisme), Analyse de séquence de protéine (MeSH), Animaux (MeSH), Cadres ouverts de lecture (physiologie), Clonage moléculaire (MeSH), Coléoptères (enzymologie), Coléoptères (génétique), Données de séquences moléculaires (MeSH), Escherichia coli (génétique), Flavine adénine dinucléotide (métabolisme), Glucosides (MeSH), Larve (enzymologie), Larve (génétique), Populus (MeSH), Protéines d'insecte (génétique), Protéines d'insecte (métabolisme), Salix (MeSH), Signaux de triage des protéines (physiologie), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (physiologie), Séquence d'acides aminés (MeSH).
- MESH :
- enzymologie : Coléoptères, Larve.
- génétique : Alcohol oxidoreductases, Coléoptères, Escherichia coli, Larve, Protéines d'insecte.
- métabolisme : Alcohol oxidoreductases, Alcools benzyliques, Aldéhydes, Flavine adénine dinucléotide, Protéines d'insecte.
- physiologie : Cadres ouverts de lecture, Signaux de triage des protéines, Sites de fixation.
- Analyse de séquence de protéine, Animaux, Clonage moléculaire, Données de séquences moléculaires, Glucosides, Populus, Salix, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (genetics), Alcohol Oxidoreductases (metabolism), Aldehydes (metabolism), Amino Acid Sequence (MeSH), Animals (MeSH), Benzyl Alcohols (metabolism), Binding Sites (physiology), Cloning, Molecular (MeSH), Coleoptera (enzymology), Coleoptera (genetics), Escherichia coli (genetics), Flavin-Adenine Dinucleotide (metabolism), Glucosides (MeSH), Insect Proteins (genetics), Insect Proteins (metabolism), Larva (enzymology), Larva (genetics), Molecular Sequence Data (MeSH), Open Reading Frames (physiology), Populus (MeSH), Protein Sorting Signals (physiology), Salix (MeSH), Sequence Analysis, Protein (MeSH), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , genetics : Alcohol Oxidoreductases, Insect Proteins.
- chemical , metabolism : Alcohol Oxidoreductases, Aldehydes, Benzyl Alcohols, Flavin-Adenine Dinucleotide, Insect Proteins.
- enzymology : Coleoptera, Larva.
- genetics : Coleoptera, Escherichia coli, Larva.
- physiology : Binding Sites, Open Reading Frames, Protein Sorting Signals.
- Amino Acid Sequence, Animals, Cloning, Molecular, Glucosides, Molecular Sequence Data, Populus, Salix, Sequence Analysis, Protein, Sequence Homology, Amino Acid.
Abstract
Salicyl alcohol oxidase is an extracellular enzyme that occurs in glandular reservoirs of chrysomelid leaf beetle larvae and catalyzes the formation of salicylaldehyde, a volatile deterrent used by the larvae against predators. Salicyl alcohol is the hydrolysis product of salicin, a plant-derived precursor taken up by the beetle larvae from the leaves of willow and poplar trees. The cDNA encoding salicyl alcohol oxidase from two related species Chrysomela tremulae and Chrysomela populi has been identified, cloned, and expressed in an active form in Escherichia coli. The open reading frame of 623 amino acids begins in both enzymes with an N-terminal signal peptide of 21 amino acids. Sequence comparison has revealed that salicyl alcohol oxidase belongs to the family of glucose-methanol-choline oxidoreductase-like sequences with mostly unknown function. Enzymes of this family share similar overall structure with an essentially identical FAD-binding site but possess different catalytic activities. The data suggest that salicyl alcohol oxidase, essential for the activation of the plant-derived precursor salicin, was originally recruited from an oxidase involved in the autogenous biosynthesis of iridoid monoterpenes and found in related chrysomelid leaf beetle species.
DOI: 10.1074/jbc.M802236200
PubMed: 18482980
Affiliations:
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(genetics)</term><term>Escherichia coli (genetics)</term><term>Flavin-Adenine Dinucleotide (metabolism)</term><term>Glucosides (MeSH)</term><term>Insect Proteins (genetics)</term><term>Insect Proteins (metabolism)</term><term>Larva (enzymology)</term><term>Larva (genetics)</term><term>Molecular Sequence Data (MeSH)</term><term>Open Reading Frames (physiology)</term><term>Populus (MeSH)</term><term>Protein Sorting Signals (physiology)</term><term>Salix (MeSH)</term><term>Sequence Analysis, Protein (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcohol oxidoreductases (génétique)</term><term>Alcohol oxidoreductases (métabolisme)</term><term>Alcools benzyliques (métabolisme)</term><term>Aldéhydes (métabolisme)</term><term>Analyse de séquence de protéine (MeSH)</term><term>Animaux (MeSH)</term><term>Cadres ouverts de lecture (physiologie)</term><term>Clonage moléculaire (MeSH)</term><term>Coléoptères (enzymologie)</term><term>Coléoptères (génétique)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (génétique)</term><term>Flavine adénine dinucléotide (métabolisme)</term><term>Glucosides (MeSH)</term><term>Larve (enzymologie)</term><term>Larve (génétique)</term><term>Populus (MeSH)</term><term>Protéines d'insecte (génétique)</term><term>Protéines d'insecte (métabolisme)</term><term>Salix (MeSH)</term><term>Signaux de triage des protéines (physiologie)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Sites de fixation (physiologie)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Insect Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Aldehydes</term><term>Benzyl Alcohols</term><term>Flavin-Adenine Dinucleotide</term><term>Insect Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Coléoptères</term><term>Larve</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Coleoptera</term><term>Larva</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Coleoptera</term><term>Escherichia coli</term><term>Larva</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Coléoptères</term><term>Escherichia coli</term><term>Larve</term><term>Protéines d'insecte</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Alcools benzyliques</term><term>Aldéhydes</term><term>Flavine adénine dinucléotide</term><term>Protéines d'insecte</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cadres ouverts de lecture</term><term>Signaux de triage des protéines</term><term>Sites de fixation</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Binding Sites</term><term>Open Reading Frames</term><term>Protein Sorting Signals</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cloning, Molecular</term><term>Glucosides</term><term>Molecular Sequence Data</term><term>Populus</term><term>Salix</term><term>Sequence Analysis, Protein</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence de protéine</term><term>Animaux</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Glucosides</term><term>Populus</term><term>Salix</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Salicyl alcohol oxidase is an extracellular enzyme that occurs in glandular reservoirs of chrysomelid leaf beetle larvae and catalyzes the formation of salicylaldehyde, a volatile deterrent used by the larvae against predators. Salicyl alcohol is the hydrolysis product of salicin, a plant-derived precursor taken up by the beetle larvae from the leaves of willow and poplar trees. The cDNA encoding salicyl alcohol oxidase from two related species Chrysomela tremulae and Chrysomela populi has been identified, cloned, and expressed in an active form in Escherichia coli. The open reading frame of 623 amino acids begins in both enzymes with an N-terminal signal peptide of 21 amino acids. Sequence comparison has revealed that salicyl alcohol oxidase belongs to the family of glucose-methanol-choline oxidoreductase-like sequences with mostly unknown function. Enzymes of this family share similar overall structure with an essentially identical FAD-binding site but possess different catalytic activities. The data suggest that salicyl alcohol oxidase, essential for the activation of the plant-derived precursor salicin, was originally recruited from an oxidase involved in the autogenous biosynthesis of iridoid monoterpenes and found in related chrysomelid leaf beetle species.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18482980</PMID><DateCompleted><Year>2008</Year><Month>08</Month><Day>28</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>283</Volume><Issue>28</Issue><PubDate><Year>2008</Year><Month>Jul</Month><Day>11</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Salicyl alcohol oxidase of the chemical defense secretion of two chrysomelid leaf beetles. Molecular and functional characterization of two new members of the glucose-methanol-choline oxidoreductase gene family.</ArticleTitle><Pagination><MedlinePgn>19219-28</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M802236200</ELocationID><Abstract><AbstractText>Salicyl alcohol oxidase is an extracellular enzyme that occurs in glandular reservoirs of chrysomelid leaf beetle larvae and catalyzes the formation of salicylaldehyde, a volatile deterrent used by the larvae against predators. Salicyl alcohol is the hydrolysis product of salicin, a plant-derived precursor taken up by the beetle larvae from the leaves of willow and poplar trees. The cDNA encoding salicyl alcohol oxidase from two related species Chrysomela tremulae and Chrysomela populi has been identified, cloned, and expressed in an active form in Escherichia coli. The open reading frame of 623 amino acids begins in both enzymes with an N-terminal signal peptide of 21 amino acids. Sequence comparison has revealed that salicyl alcohol oxidase belongs to the family of glucose-methanol-choline oxidoreductase-like sequences with mostly unknown function. Enzymes of this family share similar overall structure with an essentially identical FAD-binding site but possess different catalytic activities. The data suggest that salicyl alcohol oxidase, essential for the activation of the plant-derived precursor salicin, was originally recruited from an oxidase involved in the autogenous biosynthesis of iridoid monoterpenes and found in related chrysomelid leaf beetle species.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Michalski</LastName><ForeName>Carmen</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Botanisches Institut und Botanischer Garten, Universität Kiel, Olshausenstrasse 40, 24098 Kiel, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mohagheghi</LastName><ForeName>Hoda</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Nimtz</LastName><ForeName>Manfred</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Pasteels</LastName><ForeName>Jacques</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Ober</LastName><ForeName>Dietrich</ForeName><Initials>D</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AM947503</AccessionNumber><AccessionNumber>AM947504</AccessionNumber><AccessionNumber>AM947505</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>05</Month><Day>15</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000447">Aldehydes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005960">Glucosides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019476">Insect Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D021382">Protein Sorting Signals</NameOfSubstance></Chemical><Chemical><RegistryNumber>146-14-5</RegistryNumber><NameOfSubstance UI="D005182">Flavin-Adenine Dinucleotide</NameOfSubstance></Chemical><Chemical><RegistryNumber>17K64GZH20</RegistryNumber><NameOfSubstance UI="C013243">salicylaldehyde</NameOfSubstance></Chemical><Chemical><RegistryNumber>4649620TBZ</RegistryNumber><NameOfSubstance UI="C005696">salicin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.7</RegistryNumber><NameOfSubstance UI="C473419">salicyl alcohol oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>FA1N0842KB</RegistryNumber><NameOfSubstance UI="C010631">salicyl alcohol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000429" MajorTopicYN="N">Alcohol Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000447" MajorTopicYN="N">Aldehydes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001517" MajorTopicYN="N">Coleoptera</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005182" MajorTopicYN="N">Flavin-Adenine Dinucleotide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005960" MajorTopicYN="N">Glucosides</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019476" MajorTopicYN="N">Insect Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007814" MajorTopicYN="N">Larva</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016366" MajorTopicYN="N">Open Reading Frames</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021382" MajorTopicYN="N">Protein Sorting Signals</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032108" MajorTopicYN="N">Salix</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020539" MajorTopicYN="N">Sequence Analysis, Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>5</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>8</Month><Day>30</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>5</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18482980</ArticleId><ArticleId IdType="pii">M802236200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M802236200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Schleswig-Holstein</li></region><settlement><li>Kiel</li></settlement></list><tree><noCountry><name sortKey="Mohagheghi, Hoda" sort="Mohagheghi, Hoda" uniqKey="Mohagheghi H" first="Hoda" last="Mohagheghi">Hoda Mohagheghi</name><name sortKey="Nimtz, Manfred" sort="Nimtz, Manfred" uniqKey="Nimtz M" first="Manfred" last="Nimtz">Manfred Nimtz</name><name sortKey="Ober, Dietrich" sort="Ober, Dietrich" uniqKey="Ober D" first="Dietrich" last="Ober">Dietrich Ober</name><name sortKey="Pasteels, Jacques" sort="Pasteels, Jacques" uniqKey="Pasteels J" first="Jacques" last="Pasteels">Jacques Pasteels</name></noCountry><country name="Allemagne"><region name="Schleswig-Holstein"><name sortKey="Michalski, Carmen" sort="Michalski, Carmen" uniqKey="Michalski C" first="Carmen" last="Michalski">Carmen Michalski</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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