Biochemical characterization, cDNA cloning and protein crystallization of aryl-alcohol oxidase from Pleurotus pulmonarius.
Identifieur interne : 000B02 ( Main/Exploration ); précédent : 000B01; suivant : 000B03Biochemical characterization, cDNA cloning and protein crystallization of aryl-alcohol oxidase from Pleurotus pulmonarius.
Auteurs : E. Varela [Espagne] ; B. Böckle ; A. Romero ; A T Martínez ; M J MartínezSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2000.
Descripteurs français
- KwdFr :
- ADN complémentaire (composition chimique), Alcohol oxidoreductases (composition chimique), Alcohol oxidoreductases (génétique), Alcohol oxidoreductases (métabolisme), Cinétique (MeSH), Clonage moléculaire (MeSH), Cristallisation (MeSH), Données de séquences moléculaires (MeSH), Masse moléculaire (MeSH), Pleurotus (enzymologie), Pleurotus (génétique), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : ADN complémentaire, Alcohol oxidoreductases, Protéines fongiques.
- enzymologie : Pleurotus.
- génétique : Alcohol oxidoreductases, Pleurotus, Protéines fongiques.
- métabolisme : Alcohol oxidoreductases, Protéines fongiques.
- Cinétique, Clonage moléculaire, Cristallisation, Données de séquences moléculaires, Masse moléculaire, Spécificité du substrat, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (chemistry), Alcohol Oxidoreductases (genetics), Alcohol Oxidoreductases (metabolism), Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), Crystallization (MeSH), DNA, Complementary (chemistry), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Kinetics (MeSH), Molecular Sequence Data (MeSH), Molecular Weight (MeSH), Pleurotus (enzymology), Pleurotus (genetics), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Alcohol Oxidoreductases, DNA, Complementary, Fungal Proteins.
- chemical , genetics : Alcohol Oxidoreductases, Fungal Proteins.
- chemical , metabolism : Alcohol Oxidoreductases, Fungal Proteins.
- enzymology : Pleurotus.
- genetics : Pleurotus.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Crystallization, Kinetics, Molecular Sequence Data, Molecular Weight, Substrate Specificity.
Abstract
Aryl-alcohol oxidase (AAO) involved in lignin degradation by Pleurotus pulmonarius has been purified and characterized. The enzyme was produced in glucose-peptone medium and isolated in a sole chromatographic step using Sephacryl S-200. The purified enzyme is an extracellular glycoprotein with 14% N-carbohydrate content and an estimated molecular mass of 70.5 kDa and pI of 3.95. The kinetic studies showed the highest enzyme affinity against p-anisyl alcohol, with constants similar to those of Pleurotus eryngii and Bjerkandera adusta AAO but different from the intracellular AAO described in Phanerochaete chrysosporium, which present the highest activity on m-anisyl alcohol. Simultaneously, the cDNA of P. pulmonarius AAO has been cloned and sequenced. The translation of this sequence consisted of 593 amino acids including a signal peptide of 27 amino acids. The comparison with other alcohol oxidases, 35% amino acid identity with glucose oxidase, showed highly conserved amino acid sequences in N-terminal and C-terminal regions, in spite of differences in substrate specificity. Crystallization of AAO, carried out for the first time using the P. pulmonarius enzyme, will permit to obtain a molecular model for this oxidase and establish some characteristic of its catalytic site and general structure.
DOI: 10.1016/s0167-4838(99)00227-7
PubMed: 10606774
Affiliations:
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Varela</name><affiliation wicri:level="3"><nlm:affiliation>Centro de Investigaciones Biológicas, CSIC, Velázquez 144, E-28006, Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Centro de Investigaciones Biológicas, CSIC, Velázquez 144, E-28006, Madrid</wicri:regionArea><placeName><settlement type="city">Madrid</settlement><region nuts="2" type="region">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="Bockle, B" sort="Bockle, B" uniqKey="Bockle B" first="B" last="Böckle">B. Böckle</name></author><author><name sortKey="Romero, A" sort="Romero, A" uniqKey="Romero A" first="A" last="Romero">A. 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The enzyme was produced in glucose-peptone medium and isolated in a sole chromatographic step using Sephacryl S-200. The purified enzyme is an extracellular glycoprotein with 14% N-carbohydrate content and an estimated molecular mass of 70.5 kDa and pI of 3.95. The kinetic studies showed the highest enzyme affinity against p-anisyl alcohol, with constants similar to those of Pleurotus eryngii and Bjerkandera adusta AAO but different from the intracellular AAO described in Phanerochaete chrysosporium, which present the highest activity on m-anisyl alcohol. Simultaneously, the cDNA of P. pulmonarius AAO has been cloned and sequenced. The translation of this sequence consisted of 593 amino acids including a signal peptide of 27 amino acids. The comparison with other alcohol oxidases, 35% amino acid identity with glucose oxidase, showed highly conserved amino acid sequences in N-terminal and C-terminal regions, in spite of differences in substrate specificity. Crystallization of AAO, carried out for the first time using the P. pulmonarius enzyme, will permit to obtain a molecular model for this oxidase and establish some characteristic of its catalytic site and general structure.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10606774</PMID><DateCompleted><Year>2000</Year><Month>03</Month><Day>23</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1476</Volume><Issue>1</Issue><PubDate><Year>2000</Year><Month>Jan</Month><Day>03</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Biochemical characterization, cDNA cloning and protein crystallization of aryl-alcohol oxidase from Pleurotus pulmonarius.</ArticleTitle><Pagination><MedlinePgn>129-38</MedlinePgn></Pagination><Abstract><AbstractText>Aryl-alcohol oxidase (AAO) involved in lignin degradation by Pleurotus pulmonarius has been purified and characterized. The enzyme was produced in glucose-peptone medium and isolated in a sole chromatographic step using Sephacryl S-200. The purified enzyme is an extracellular glycoprotein with 14% N-carbohydrate content and an estimated molecular mass of 70.5 kDa and pI of 3.95. The kinetic studies showed the highest enzyme affinity against p-anisyl alcohol, with constants similar to those of Pleurotus eryngii and Bjerkandera adusta AAO but different from the intracellular AAO described in Phanerochaete chrysosporium, which present the highest activity on m-anisyl alcohol. Simultaneously, the cDNA of P. pulmonarius AAO has been cloned and sequenced. The translation of this sequence consisted of 593 amino acids including a signal peptide of 27 amino acids. The comparison with other alcohol oxidases, 35% amino acid identity with glucose oxidase, showed highly conserved amino acid sequences in N-terminal and C-terminal regions, in spite of differences in substrate specificity. Crystallization of AAO, carried out for the first time using the P. pulmonarius enzyme, will permit to obtain a molecular model for this oxidase and establish some characteristic of its catalytic site and general structure.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Varela</LastName><ForeName>E</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Centro de Investigaciones Biológicas, CSIC, Velázquez 144, E-28006, Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Böckle</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Romero</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Martínez</LastName><ForeName>A T</ForeName><Initials>AT</Initials></Author><Author ValidYN="Y"><LastName>Martínez</LastName><ForeName>M J</ForeName><Initials>MJ</Initials></Author></AuthorList><Language>eng</Language><DataBankList 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Böckle</name><name sortKey="Martinez, A T" sort="Martinez, A T" uniqKey="Martinez A" first="A T" last="Martínez">A T Martínez</name><name sortKey="Martinez, M J" sort="Martinez, M J" uniqKey="Martinez M" first="M J" last="Martínez">M J Martínez</name><name sortKey="Romero, A" sort="Romero, A" uniqKey="Romero A" first="A" last="Romero">A. Romero</name></noCountry><country name="Espagne"><region name="Communauté de Madrid"><name sortKey="Varela, E" sort="Varela, E" uniqKey="Varela E" first="E" last="Varela">E. Varela</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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