A beta-glucosidase/xylosidase from the phytopathogenic oomycete, Phytophthora infestans.
Identifieur interne : 002696 ( Main/Corpus ); précédent : 002695; suivant : 002697A beta-glucosidase/xylosidase from the phytopathogenic oomycete, Phytophthora infestans.
Auteurs : Frédéric Brunner ; Wolfgang Wirtz ; Jocelyn K C. Rose ; Alan G. Darvill ; Francine Govers ; Dierk Scheel ; Thorsten NürnbergerSource :
- Phytochemistry [ 0031-9422 ] ; 2002.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Bacterial Proteins (MeSH), Base Sequence (MeSH), DNA, Fungal (analysis), Glucosides (metabolism), Glucosylceramidase (genetics), Glycoside Hydrolases (metabolism), Humans (MeSH), Hymecromone (analogs & derivatives), Hymecromone (metabolism), Mice (MeSH), Molecular Sequence Data (MeSH), Oomycetes (enzymology), Species Specificity (MeSH), Substrate Specificity (MeSH), Xylosidases (genetics), Xylosidases (isolation & purification), Xylosidases (metabolism), beta-Glucosidase (genetics), beta-Glucosidase (isolation & purification), beta-Glucosidase (metabolism).
- MESH :
- chemical , analogs & derivatives : Hymecromone.
- chemical , analysis : DNA, Fungal.
- chemical , genetics : Glucosylceramidase, Xylosidases, beta-Glucosidase.
- chemical , isolation & purification : Xylosidases, beta-Glucosidase.
- chemical , metabolism : Glucosides, Glycoside Hydrolases, Hymecromone, Xylosidases, beta-Glucosidase.
- chemical : Bacterial Proteins.
- enzymology : Oomycetes.
- Amino Acid Sequence, Animals, Base Sequence, Humans, Mice, Molecular Sequence Data, Species Specificity, Substrate Specificity.
Abstract
An 85-kDa beta-glucosidase/xylosidase (BGX1) was purified from the axenically grown phytopathogenic oomycete, Phytophthora infestans. The bgx1 gene encodes a predicted 61-kDa protein product which, upon removal of a 21 amino acid leader peptide, accumulates in the apoplastic space. Extensive N-mannosylation accounts for part of the observed molecular mass difference. BGX1 belongs to family 30 of the glycoside hydrolases and is the first such oomycete enzyme deposited in public databases. The bgx1 gene was found in various Phytophthora species, but is apparently absent in species of the related genus, Pythium. Despite significant sequence similarity to human and murine lysosomal glucosylceramidases, BGX1 demonstrated neither glucocerebroside nor galactocerebroside-hydrolyzing activity. The native enzyme exhibited glucohydrolytic activity towards 4-methylumbelliferyl (4-MU) beta-D-glucopyranoside and, to lesser extent, towards 4-MU-D-xylopyranoside, but not towards 4-MU-beta-D-glucopyranoside. BGX1 did not hydrolyze carboxymethyl cellulose, cellotetraose, chitosan or xylan, suggesting high substrate specificity and/or specific cofactor requirements for enzymatic activity.
DOI: 10.1016/s0031-9422(02)00045-6
PubMed: 11909624
Links to Exploration step
pubmed:11909624Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A beta-glucosidase/xylosidase from the phytopathogenic oomycete, Phytophthora infestans.</title><author><name sortKey="Brunner, Frederic" sort="Brunner, Frederic" uniqKey="Brunner F" first="Frédéric" last="Brunner">Frédéric Brunner</name><affiliation><nlm:affiliation>Institut für Pflanzenbiochemie, Abteilung Stress- und Entwicklungsbiologie, Weinberg 3, D-06120, Halle/Saale, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Wirtz, Wolfgang" sort="Wirtz, Wolfgang" uniqKey="Wirtz W" first="Wolfgang" last="Wirtz">Wolfgang Wirtz</name></author><author><name sortKey="Rose, Jocelyn K C" sort="Rose, Jocelyn K C" uniqKey="Rose J" first="Jocelyn K C" last="Rose">Jocelyn K C. Rose</name></author><author><name sortKey="Darvill, Alan G" sort="Darvill, Alan G" uniqKey="Darvill A" first="Alan G" last="Darvill">Alan G. Darvill</name></author><author><name sortKey="Govers, Francine" sort="Govers, Francine" uniqKey="Govers F" first="Francine" last="Govers">Francine Govers</name></author><author><name sortKey="Scheel, Dierk" sort="Scheel, Dierk" uniqKey="Scheel D" first="Dierk" last="Scheel">Dierk Scheel</name></author><author><name sortKey="Nurnberger, Thorsten" sort="Nurnberger, Thorsten" uniqKey="Nurnberger T" first="Thorsten" last="Nürnberger">Thorsten Nürnberger</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:11909624</idno><idno type="pmid">11909624</idno><idno type="doi">10.1016/s0031-9422(02)00045-6</idno><idno type="wicri:Area/Main/Corpus">002696</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002696</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A beta-glucosidase/xylosidase from the phytopathogenic oomycete, Phytophthora infestans.</title><author><name sortKey="Brunner, Frederic" sort="Brunner, Frederic" uniqKey="Brunner F" first="Frédéric" last="Brunner">Frédéric Brunner</name><affiliation><nlm:affiliation>Institut für Pflanzenbiochemie, Abteilung Stress- und Entwicklungsbiologie, Weinberg 3, D-06120, Halle/Saale, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Wirtz, Wolfgang" sort="Wirtz, Wolfgang" uniqKey="Wirtz W" first="Wolfgang" last="Wirtz">Wolfgang Wirtz</name></author><author><name sortKey="Rose, Jocelyn K C" sort="Rose, Jocelyn K C" uniqKey="Rose J" first="Jocelyn K C" last="Rose">Jocelyn K C. Rose</name></author><author><name sortKey="Darvill, Alan G" sort="Darvill, Alan G" uniqKey="Darvill A" first="Alan G" last="Darvill">Alan G. Darvill</name></author><author><name sortKey="Govers, Francine" sort="Govers, Francine" uniqKey="Govers F" first="Francine" last="Govers">Francine Govers</name></author><author><name sortKey="Scheel, Dierk" sort="Scheel, Dierk" uniqKey="Scheel D" first="Dierk" last="Scheel">Dierk Scheel</name></author><author><name sortKey="Nurnberger, Thorsten" sort="Nurnberger, Thorsten" uniqKey="Nurnberger T" first="Thorsten" last="Nürnberger">Thorsten Nürnberger</name></author></analytic><series><title level="j">Phytochemistry</title><idno type="ISSN">0031-9422</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Bacterial Proteins (MeSH)</term><term>Base Sequence (MeSH)</term><term>DNA, Fungal (analysis)</term><term>Glucosides (metabolism)</term><term>Glucosylceramidase (genetics)</term><term>Glycoside Hydrolases (metabolism)</term><term>Humans (MeSH)</term><term>Hymecromone (analogs & derivatives)</term><term>Hymecromone (metabolism)</term><term>Mice (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oomycetes (enzymology)</term><term>Species Specificity (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Xylosidases (genetics)</term><term>Xylosidases (isolation & purification)</term><term>Xylosidases (metabolism)</term><term>beta-Glucosidase (genetics)</term><term>beta-Glucosidase (isolation & purification)</term><term>beta-Glucosidase (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Hymecromone</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>DNA, Fungal</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glucosylceramidase</term><term>Xylosidases</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Xylosidases</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glucosides</term><term>Glycoside Hydrolases</term><term>Hymecromone</term><term>Xylosidases</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Bacterial Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Oomycetes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Humans</term><term>Mice</term><term>Molecular Sequence Data</term><term>Species Specificity</term><term>Substrate Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">An 85-kDa beta-glucosidase/xylosidase (BGX1) was purified from the axenically grown phytopathogenic oomycete, Phytophthora infestans. The bgx1 gene encodes a predicted 61-kDa protein product which, upon removal of a 21 amino acid leader peptide, accumulates in the apoplastic space. Extensive N-mannosylation accounts for part of the observed molecular mass difference. BGX1 belongs to family 30 of the glycoside hydrolases and is the first such oomycete enzyme deposited in public databases. The bgx1 gene was found in various Phytophthora species, but is apparently absent in species of the related genus, Pythium. Despite significant sequence similarity to human and murine lysosomal glucosylceramidases, BGX1 demonstrated neither glucocerebroside nor galactocerebroside-hydrolyzing activity. The native enzyme exhibited glucohydrolytic activity towards 4-methylumbelliferyl (4-MU) beta-D-glucopyranoside and, to lesser extent, towards 4-MU-D-xylopyranoside, but not towards 4-MU-beta-D-glucopyranoside. BGX1 did not hydrolyze carboxymethyl cellulose, cellotetraose, chitosan or xylan, suggesting high substrate specificity and/or specific cofactor requirements for enzymatic activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11909624</PMID><DateCompleted><Year>2002</Year><Month>09</Month><Day>12</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0031-9422</ISSN><JournalIssue CitedMedium="Print"><Volume>59</Volume><Issue>7</Issue><PubDate><Year>2002</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Phytochemistry</Title><ISOAbbreviation>Phytochemistry</ISOAbbreviation></Journal><ArticleTitle>A beta-glucosidase/xylosidase from the phytopathogenic oomycete, Phytophthora infestans.</ArticleTitle><Pagination><MedlinePgn>689-96</MedlinePgn></Pagination><Abstract><AbstractText>An 85-kDa beta-glucosidase/xylosidase (BGX1) was purified from the axenically grown phytopathogenic oomycete, Phytophthora infestans. The bgx1 gene encodes a predicted 61-kDa protein product which, upon removal of a 21 amino acid leader peptide, accumulates in the apoplastic space. Extensive N-mannosylation accounts for part of the observed molecular mass difference. BGX1 belongs to family 30 of the glycoside hydrolases and is the first such oomycete enzyme deposited in public databases. The bgx1 gene was found in various Phytophthora species, but is apparently absent in species of the related genus, Pythium. Despite significant sequence similarity to human and murine lysosomal glucosylceramidases, BGX1 demonstrated neither glucocerebroside nor galactocerebroside-hydrolyzing activity. The native enzyme exhibited glucohydrolytic activity towards 4-methylumbelliferyl (4-MU) beta-D-glucopyranoside and, to lesser extent, towards 4-MU-D-xylopyranoside, but not towards 4-MU-beta-D-glucopyranoside. BGX1 did not hydrolyze carboxymethyl cellulose, cellotetraose, chitosan or xylan, suggesting high substrate specificity and/or specific cofactor requirements for enzymatic activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Brunner</LastName><ForeName>Frédéric</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Institut für Pflanzenbiochemie, Abteilung Stress- und Entwicklungsbiologie, Weinberg 3, D-06120, Halle/Saale, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wirtz</LastName><ForeName>Wolfgang</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Rose</LastName><ForeName>Jocelyn K C</ForeName><Initials>JK</Initials></Author><Author ValidYN="Y"><LastName>Darvill</LastName><ForeName>Alan G</ForeName><Initials>AG</Initials></Author><Author ValidYN="Y"><LastName>Govers</LastName><ForeName>Francine</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Scheel</LastName><ForeName>Dierk</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Nürnberger</LastName><ForeName>Thorsten</ForeName><Initials>T</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Phytochemistry</MedlineTA><NlmUniqueID>0151434</NlmUniqueID><ISSNLinking>0031-9422</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004271">DNA, Fungal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005960">Glucosides</NameOfSubstance></Chemical><Chemical><RegistryNumber>18997-57-4</RegistryNumber><NameOfSubstance UI="C014110">4-methylumbelliferyl glucoside</NameOfSubstance></Chemical><Chemical><RegistryNumber>3T5NG4Q468</RegistryNumber><NameOfSubstance UI="D006923">Hymecromone</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D006026">Glycoside Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D014995">Xylosidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.21</RegistryNumber><NameOfSubstance UI="D001617">beta-Glucosidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.37</RegistryNumber><NameOfSubstance UI="C092512">BgxA protein, Erwinia chrysanthemi</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.45</RegistryNumber><NameOfSubstance UI="D005962">Glucosylceramidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="Y">Bacterial Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004271" MajorTopicYN="N">DNA, Fungal</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005960" MajorTopicYN="N">Glucosides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005962" MajorTopicYN="N">Glucosylceramidase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006026" MajorTopicYN="N">Glycoside Hydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006923" MajorTopicYN="N">Hymecromone</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009868" MajorTopicYN="N">Oomycetes</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013045" MajorTopicYN="N">Species Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014995" MajorTopicYN="N">Xylosidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001617" MajorTopicYN="N">beta-Glucosidase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>3</Month><Day>23</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>9</Month><Day>13</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>3</Month><Day>23</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11909624</ArticleId><ArticleId IdType="pii">S0031942202000456</ArticleId><ArticleId IdType="doi">10.1016/s0031-9422(02)00045-6</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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