Enzymatic properties of native and deglycosylated hybrid aspen (Populus tremulaxtremuloides) xyloglucan endotransglycosylase 16A expressed in Pichia pastoris.
Identifieur interne : 004045 ( Main/Exploration ); précédent : 004044; suivant : 004046Enzymatic properties of native and deglycosylated hybrid aspen (Populus tremulaxtremuloides) xyloglucan endotransglycosylase 16A expressed in Pichia pastoris.
Auteurs : Asa M. Kallas [Suède] ; Kathleen Piens ; Stuart E. Denman ; Hongbin Henriksson ; Jenny F Ldt ; Patrik Johansson ; Harry Brumer ; Tuula T. TeeriSource :
- The Biochemical journal [ 1470-8728 ] ; 2005.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Concentration en ions d'hydrogène (MeSH), Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Dénaturation des protéines (MeSH), Expression des gènes (physiologie), Glycosyltransferase (composition chimique), Glycosyltransferase (génétique), Glycosyltransferase (métabolisme), Isoformes de protéines (MeSH), Mutation (MeSH), Pichia (métabolisme), Populus (enzymologie), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Stabilité enzymatique (MeSH), Substitution d'acide aminé (MeSH), Séquence d'acides aminés (MeSH), Température (MeSH).
- MESH :
- composition chimique : Glycosyltransferase.
- enzymologie : Populus.
- génétique : Glycosyltransferase.
- métabolisme : Glycosyltransferase, Pichia.
- physiologie : Expression des gènes.
- Alignement de séquences, Concentration en ions d'hydrogène, Conformation des protéines, Données de séquences moléculaires, Dénaturation des protéines, Isoformes de protéines, Mutation, Similitude de séquences d'acides aminés, Sites de fixation, Stabilité enzymatique, Substitution d'acide aminé, Séquence d'acides aminés, Température.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Amino Acid Substitution (MeSH), Binding Sites (MeSH), Enzyme Stability (MeSH), Gene Expression (physiology), Glycosyltransferases (chemistry), Glycosyltransferases (genetics), Glycosyltransferases (metabolism), Hydrogen-Ion Concentration (MeSH), Molecular Sequence Data (MeSH), Mutation (MeSH), Pichia (metabolism), Populus (enzymology), Protein Conformation (MeSH), Protein Denaturation (MeSH), Protein Isoforms (MeSH), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Temperature (MeSH).
- MESH :
- chemical , chemistry : Glycosyltransferases.
- chemical , genetics : Glycosyltransferases.
- chemical , metabolism : Glycosyltransferases.
- enzymology : Populus.
- metabolism : Pichia.
- physiology : Gene Expression.
- Amino Acid Sequence, Amino Acid Substitution, Binding Sites, Enzyme Stability, Hydrogen-Ion Concentration, Molecular Sequence Data, Mutation, Protein Conformation, Protein Denaturation, Protein Isoforms, Sequence Alignment, Sequence Homology, Amino Acid, Temperature.
Abstract
The cDNA encoding a xyloglucan endotransglycosylase, PttXET16A, from hybrid aspen (Populus tremulaxtremuloides) has been isolated from an expressed sequence tag library and expressed in the methylotrophic yeast Pichia pastoris. Sequence analysis indicated a high degree of similarity with other proteins in the XTH (xyloglucan transglycosylase/hydrolase) gene subfamily of GH16 (glycoside hydrolase family 16). In addition to the conserved GH16 catalytic sequence motif, PttXET16A contains a conserved N-glycosylation site situated proximal to the predicted catalytic residues. MS analysis indicated that the recombinant PttXET16A expressed in P. pastoris is heterogeneous due to the presence of variable N-glycosylation and incomplete cleavage of the alpha-factor secretion signal peptide. Removal of the N-glycan by endoglycosidase H treatment did not influence the catalytic activity significantly. Similarly, site-directed mutagenesis of Asn93 to serine to remove the N-glycosylation site resulted in an enzyme which was comparable with the wild-type enzyme in specific activity and thermal stability but had clearly reduced solubility. Hydrolytic activity was detected neither in wild-type PttXET16A before or after enzymatic deglycosylation nor in PttXET16A N93S (Asn93-->Ser) mutant.
DOI: 10.1042/BJ20041749
PubMed: 15804235
PubMed Central: PMC1184566
Affiliations:
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Sequence analysis indicated a high degree of similarity with other proteins in the XTH (xyloglucan transglycosylase/hydrolase) gene subfamily of GH16 (glycoside hydrolase family 16). In addition to the conserved GH16 catalytic sequence motif, PttXET16A contains a conserved N-glycosylation site situated proximal to the predicted catalytic residues. MS analysis indicated that the recombinant PttXET16A expressed in P. pastoris is heterogeneous due to the presence of variable N-glycosylation and incomplete cleavage of the alpha-factor secretion signal peptide. Removal of the N-glycan by endoglycosidase H treatment did not influence the catalytic activity significantly. Similarly, site-directed mutagenesis of Asn93 to serine to remove the N-glycosylation site resulted in an enzyme which was comparable with the wild-type enzyme in specific activity and thermal stability but had clearly reduced solubility. Hydrolytic activity was detected neither in wild-type PttXET16A before or after enzymatic deglycosylation nor in PttXET16A N93S (Asn93-->Ser) mutant.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15804235</PMID><DateCompleted><Year>2005</Year><Month>11</Month><Day>07</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1470-8728</ISSN><JournalIssue CitedMedium="Internet"><Volume>390</Volume><Issue>Pt 1</Issue><PubDate><Year>2005</Year><Month>Aug</Month><Day>15</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Enzymatic properties of native and deglycosylated hybrid aspen (Populus tremulaxtremuloides) xyloglucan endotransglycosylase 16A expressed in Pichia pastoris.</ArticleTitle><Pagination><MedlinePgn>105-13</MedlinePgn></Pagination><Abstract><AbstractText>The cDNA encoding a xyloglucan endotransglycosylase, PttXET16A, from hybrid aspen (Populus tremulaxtremuloides) has been isolated from an expressed sequence tag library and expressed in the methylotrophic yeast Pichia pastoris. Sequence analysis indicated a high degree of similarity with other proteins in the XTH (xyloglucan transglycosylase/hydrolase) gene subfamily of GH16 (glycoside hydrolase family 16). In addition to the conserved GH16 catalytic sequence motif, PttXET16A contains a conserved N-glycosylation site situated proximal to the predicted catalytic residues. MS analysis indicated that the recombinant PttXET16A expressed in P. pastoris is heterogeneous due to the presence of variable N-glycosylation and incomplete cleavage of the alpha-factor secretion signal peptide. Removal of the N-glycan by endoglycosidase H treatment did not influence the catalytic activity significantly. Similarly, site-directed mutagenesis of Asn93 to serine to remove the N-glycosylation site resulted in an enzyme which was comparable with the wild-type enzyme in specific activity and thermal stability but had clearly reduced solubility. Hydrolytic activity was detected neither in wild-type PttXET16A before or after enzymatic deglycosylation nor in PttXET16A N93S (Asn93-->Ser) mutant.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kallas</LastName><ForeName>Asa M</ForeName><Initials>AM</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Royal Institute of Technology, AlbaNova University Centre, SE-10691 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Piens</LastName><ForeName>Kathleen</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Denman</LastName><ForeName>Stuart E</ForeName><Initials>SE</Initials></Author><Author ValidYN="Y"><LastName>Henriksson</LastName><ForeName>Hongbin</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Fäldt</LastName><ForeName>Jenny</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Johansson</LastName><ForeName>Patrik</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Brumer</LastName><ForeName>Harry</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Teeri</LastName><ForeName>Tuula T</ForeName><Initials>TT</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>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020033">Protein Isoforms</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.-</RegistryNumber><NameOfSubstance UI="D016695">Glycosyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.1.-</RegistryNumber><NameOfSubstance UI="C073693">xyloglucan endotransglycosylase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016695" MajorTopicYN="N">Glycosyltransferases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010843" MajorTopicYN="N">Pichia</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020033" MajorTopicYN="N">Protein Isoforms</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>4</Month><Day>5</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>11</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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sortKey="Brumer, Harry" sort="Brumer, Harry" uniqKey="Brumer H" first="Harry" last="Brumer">Harry Brumer</name><name sortKey="Denman, Stuart E" sort="Denman, Stuart E" uniqKey="Denman S" first="Stuart E" last="Denman">Stuart E. Denman</name><name sortKey="F Ldt, Jenny" sort="F Ldt, Jenny" uniqKey="F Ldt J" first="Jenny" last="F Ldt">Jenny F Ldt</name><name sortKey="Henriksson, Hongbin" sort="Henriksson, Hongbin" uniqKey="Henriksson H" first="Hongbin" last="Henriksson">Hongbin Henriksson</name><name sortKey="Johansson, Patrik" sort="Johansson, Patrik" uniqKey="Johansson P" first="Patrik" last="Johansson">Patrik Johansson</name><name sortKey="Piens, Kathleen" sort="Piens, Kathleen" uniqKey="Piens K" first="Kathleen" last="Piens">Kathleen Piens</name><name sortKey="Teeri, Tuula T" sort="Teeri, Tuula T" uniqKey="Teeri T" first="Tuula T" last="Teeri">Tuula T. Teeri</name></noCountry><country name="Suède"><noRegion><name sortKey="Kallas, Asa M" sort="Kallas, Asa M" uniqKey="Kallas A" first="Asa M" last="Kallas">Asa M. Kallas</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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