Structural and kinetic basis for substrate selectivity in Populus tremuloides sinapyl alcohol dehydrogenase.
Identifieur interne : 003F49 ( Main/Exploration ); précédent : 003F48; suivant : 003F50Structural and kinetic basis for substrate selectivity in Populus tremuloides sinapyl alcohol dehydrogenase.
Auteurs : Erin K. Bomati [États-Unis] ; Joseph P. NoelSource :
- The Plant cell [ 1040-4651 ] ; 2005.
Descripteurs français
- KwdFr :
- Acroléine (analogues et dérivés), Acroléine (métabolisme), Alcohol dehydrogenase (composition chimique), Alcohol dehydrogenase (isolement et purification), Alcohol dehydrogenase (métabolisme), Alcohol oxidoreductases (métabolisme), Cinétique (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Lignine (biosynthèse), Modèles moléculaires (MeSH), NADP (métabolisme), Populus (composition chimique), Populus (enzymologie), Sites de fixation (physiologie), Structure moléculaire (MeSH).
- MESH :
- analogues et dérivés : Acroléine.
- biosynthèse : Lignine.
- composition chimique : Alcohol dehydrogenase, Populus.
- enzymologie : Populus.
- isolement et purification : Alcohol dehydrogenase.
- métabolisme : Acroléine, Alcohol dehydrogenase, Alcohol oxidoreductases, NADP.
- physiologie : Sites de fixation.
- Cinétique, Cristallographie aux rayons X, Données de séquences moléculaires, Modèles moléculaires, Structure moléculaire.
English descriptors
- KwdEn :
- Acrolein (analogs & derivatives), Acrolein (metabolism), Alcohol Dehydrogenase (chemistry), Alcohol Dehydrogenase (isolation & purification), Alcohol Dehydrogenase (metabolism), Alcohol Oxidoreductases (metabolism), Binding Sites (physiology), Crystallography, X-Ray (MeSH), Kinetics (MeSH), Lignin (biosynthesis), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Molecular Structure (MeSH), NADP (metabolism), Populus (chemistry), Populus (enzymology).
- MESH :
- chemical , analogs & derivatives : Acrolein.
- chemical , biosynthesis : Lignin.
- chemical , chemistry : Alcohol Dehydrogenase.
- chemical , isolation & purification : Alcohol Dehydrogenase.
- chemical , metabolism : Acrolein, Alcohol Dehydrogenase, Alcohol Oxidoreductases, NADP.
- chemistry : Populus.
- enzymology : Populus.
- physiology : Binding Sites.
- Crystallography, X-Ray, Kinetics, Models, Molecular, Molecular Sequence Data, Molecular Structure.
Abstract
We describe the three-dimensional structure of sinapyl alcohol dehydrogenase (SAD) from Populus tremuloides (aspen), a member of the NADP(H)-dependent dehydrogenase family that catalyzes the last reductive step in the formation of monolignols. The active site topology revealed by the crystal structure substantiates kinetic results indicating that SAD maintains highest specificity for the substrate sinapaldehyde. We also report substantial substrate inhibition kinetics for the SAD-catalyzed reduction of hydroxycinnamaldehydes. Although SAD and classical cinnamyl alcohol dehydrogenases (CADs) catalyze the same reaction and share some sequence identity, the active site topology of SAD is strikingly different from that predicted for classical CADs. Kinetic analyses of wild-type SAD and several active site mutants demonstrate the complexity of defining determinants of substrate specificity in these enzymes. These results, along with a phylogenetic analysis, support the inclusion of SAD in a plant alcohol dehydrogenase subfamily that includes cinnamaldehyde and benzaldehyde dehydrogenases. We used the SAD three-dimensional structure to model several of these SAD-like enzymes, and although their active site topologies largely mirror that of SAD, we describe a correlation between substrate specificity and amino acid substitution patterns in their active sites. The SAD structure thus provides a framework for understanding substrate specificity in this family of enzymes and for engineering new enzyme specificities.
DOI: 10.1105/tpc.104.029983
PubMed: 15829607
PubMed Central: PMC1091777
Affiliations:
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Bomati</name><affiliation wicri:level="1"><nlm:affiliation>Jack Skirball Chemical Biology and Proteomics Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Jack Skirball Chemical Biology and Proteomics Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037</wicri:regionArea><wicri:noRegion>California 92037</wicri:noRegion></affiliation></author><author><name sortKey="Noel, Joseph P" sort="Noel, Joseph P" uniqKey="Noel J" first="Joseph P" last="Noel">Joseph P. 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The active site topology revealed by the crystal structure substantiates kinetic results indicating that SAD maintains highest specificity for the substrate sinapaldehyde. We also report substantial substrate inhibition kinetics for the SAD-catalyzed reduction of hydroxycinnamaldehydes. Although SAD and classical cinnamyl alcohol dehydrogenases (CADs) catalyze the same reaction and share some sequence identity, the active site topology of SAD is strikingly different from that predicted for classical CADs. Kinetic analyses of wild-type SAD and several active site mutants demonstrate the complexity of defining determinants of substrate specificity in these enzymes. These results, along with a phylogenetic analysis, support the inclusion of SAD in a plant alcohol dehydrogenase subfamily that includes cinnamaldehyde and benzaldehyde dehydrogenases. We used the SAD three-dimensional structure to model several of these SAD-like enzymes, and although their active site topologies largely mirror that of SAD, we describe a correlation between substrate specificity and amino acid substitution patterns in their active sites. The SAD structure thus provides a framework for understanding substrate specificity in this family of enzymes and for engineering new enzyme specificities.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15829607</PMID><DateCompleted><Year>2006</Year><Month>01</Month><Day>06</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1040-4651</ISSN><JournalIssue CitedMedium="Print"><Volume>17</Volume><Issue>5</Issue><PubDate><Year>2005</Year><Month>May</Month></PubDate></JournalIssue><Title>The Plant cell</Title><ISOAbbreviation>Plant Cell</ISOAbbreviation></Journal><ArticleTitle>Structural and kinetic basis for substrate selectivity in Populus tremuloides sinapyl alcohol dehydrogenase.</ArticleTitle><Pagination><MedlinePgn>1598-611</MedlinePgn></Pagination><Abstract><AbstractText>We describe the three-dimensional structure of sinapyl alcohol dehydrogenase (SAD) from Populus tremuloides (aspen), a member of the NADP(H)-dependent dehydrogenase family that catalyzes the last reductive step in the formation of monolignols. The active site topology revealed by the crystal structure substantiates kinetic results indicating that SAD maintains highest specificity for the substrate sinapaldehyde. We also report substantial substrate inhibition kinetics for the SAD-catalyzed reduction of hydroxycinnamaldehydes. Although SAD and classical cinnamyl alcohol dehydrogenases (CADs) catalyze the same reaction and share some sequence identity, the active site topology of SAD is strikingly different from that predicted for classical CADs. Kinetic analyses of wild-type SAD and several active site mutants demonstrate the complexity of defining determinants of substrate specificity in these enzymes. These results, along with a phylogenetic analysis, support the inclusion of SAD in a plant alcohol dehydrogenase subfamily that includes cinnamaldehyde and benzaldehyde dehydrogenases. We used the SAD three-dimensional structure to model several of these SAD-like enzymes, and although their active site topologies largely mirror that of SAD, we describe a correlation between substrate specificity and amino acid substitution patterns in their active sites. The SAD structure thus provides a framework for understanding substrate specificity in this family of enzymes and for engineering new enzyme specificities.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bomati</LastName><ForeName>Erin K</ForeName><Initials>EK</Initials><AffiliationInfo><Affiliation>Jack Skirball Chemical Biology and Proteomics Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Noel</LastName><ForeName>Joseph P</ForeName><Initials>JP</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AAK58693</AccessionNumber><AccessionNumber>AF320110</AccessionNumber><AccessionNumber>CAA48028</AccessionNumber><AccessionNumber>P31655</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>04</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Cell</MedlineTA><NlmUniqueID>9208688</NlmUniqueID><ISSNLinking>1040-4651</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>4206-58-0</RegistryNumber><NameOfSubstance UI="C075386">sinapaldehyde</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance 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Noel</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Bomati, Erin K" sort="Bomati, Erin K" uniqKey="Bomati E" first="Erin K" last="Bomati">Erin K. Bomati</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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