Expression of lignin peroxidase H8 in Escherichia coli: folding and activation of the recombinant enzyme with Ca2+ and haem.
Identifieur interne : 000C51 ( Main/Exploration ); précédent : 000C50; suivant : 000C52Expression of lignin peroxidase H8 in Escherichia coli: folding and activation of the recombinant enzyme with Ca2+ and haem.
Auteurs : W A Doyle [Royaume-Uni] ; A T SmithSource :
- The Biochemical journal [ 0264-6021 ] ; 1996.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), Activation enzymatique (MeSH), Basidiomycota (enzymologie), Calcium (métabolisme), Calcium (pharmacologie), Données de séquences moléculaires (MeSH), Escherichia coli (enzymologie), Escherichia coli (génétique), Hème (métabolisme), Hème (pharmacologie), Isoenzymes (biosynthèse), Isoenzymes (génétique), Isoenzymes (métabolisme), Peroxidases (biosynthèse), Peroxidases (génétique), Peroxidases (métabolisme), Pliage des protéines (MeSH), Protéines fongiques (biosynthèse), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Spectrophotométrie UV (MeSH), Séquence nucléotidique (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- biosynthèse : Isoenzymes, Peroxidases, Protéines fongiques.
- enzymologie : Basidiomycota, Escherichia coli.
- génétique : ADN complémentaire, Escherichia coli, Isoenzymes, Peroxidases, Protéines fongiques, Protéines recombinantes.
- métabolisme : Calcium, Hème, Isoenzymes, Peroxidases, Protéines fongiques, Protéines recombinantes.
- pharmacologie : Calcium, Hème.
- Activation enzymatique, Données de séquences moléculaires, Pliage des protéines, Spectrophotométrie UV, Séquence nucléotidique, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Base Sequence (MeSH), Basidiomycota (enzymology), Calcium (metabolism), Calcium (pharmacology), DNA, Complementary (genetics), Electrophoresis, Polyacrylamide Gel (MeSH), Enzyme Activation (MeSH), Escherichia coli (enzymology), Escherichia coli (genetics), Fungal Proteins (biosynthesis), Fungal Proteins (genetics), Fungal Proteins (metabolism), Heme (metabolism), Heme (pharmacology), Isoenzymes (biosynthesis), Isoenzymes (genetics), Isoenzymes (metabolism), Molecular Sequence Data (MeSH), Peroxidases (biosynthesis), Peroxidases (genetics), Peroxidases (metabolism), Protein Folding (MeSH), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Spectrophotometry, Ultraviolet (MeSH).
- MESH :
- chemical , biosynthesis : Fungal Proteins, Isoenzymes, Peroxidases.
- chemical , genetics : DNA, Complementary, Fungal Proteins, Isoenzymes, Peroxidases, Recombinant Proteins.
- chemical , metabolism : Calcium, Fungal Proteins, Heme, Isoenzymes, Peroxidases, Recombinant Proteins.
- enzymology : Basidiomycota, Escherichia coli.
- genetics : Escherichia coli.
- chemical , pharmacology : Calcium, Heme.
- Base Sequence, Electrophoresis, Polyacrylamide Gel, Enzyme Activation, Molecular Sequence Data, Protein Folding, Spectrophotometry, Ultraviolet.
Abstract
An engineered cDNA from Phanerochaete chrysosporium encoding both the mature and pro-sequence regions of Lip isoenzyme H8 (Lip) has been successfully overexpressed in Escherichia coli. The recombinant protein (LipP*) was sequestered in inclusion bodies. The reduced-denatured polypeptide has been purified by differential solubilization, and the active enzyme recovered after controlled in vitro refolding (albeit in low yield), by glutathione-mediated oxidation of disulphides, in a folding medium containing an intermediate concentration of urea, Ca2+, and haem. The procedure is analogous to that previously described for the production of active recombinant horseradish peroxidase (HRP-C*) from inclusion-body material. It is quite possible, therefore, that this type of procedure may be suitable for the recovery of most, if not all, active recombinant peroxidases. The resultant LipP* has spectral characteristics identical with that of the native enzyme as isolated from Phanerochaete chrysosporium. Its specific activity measured in the standard veratryl alcohol (VA) assay was 39 micromol of VA oxidized/min per mg of protein, a value which compares extremely favourably with that of the native enzyme (36 micromol of VA/min per mg). Although levels of active enzyme obtained are not yet as high as in the case of HRP-C* (1% conversion of crude inactive LipP* polypeptide into pure fully active Lip), it is envisaged that further refinement of the expression/folding/activation procedures will provide sufficient protein for biophysical characterization of both the wild-type and site-directed mutants.
DOI: 10.1042/bj3150015
PubMed: 8670100
PubMed Central: PMC1217164
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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University of Sussex, Falmer, Brighton, U.K.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>School of Biological Sciences, University of Sussex, Falmer, Brighton</wicri:regionArea><orgName type="university">Université du Sussex</orgName><placeName><settlement type="city">Brighton</settlement><settlement type="town">Falmer</settlement><region type="nation">Angleterre</region><region nuts="2" type="region">Sussex de l'Est</region></placeName></affiliation></author><author><name sortKey="Smith, A T" sort="Smith, A T" uniqKey="Smith A" first="A T" last="Smith">A T Smith</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="ISSN">0264-6021</idno><imprint><date when="1996" type="published">1996</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence (MeSH)</term><term>Basidiomycota (enzymology)</term><term>Calcium 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(génétique)</term><term>Activation enzymatique (MeSH)</term><term>Basidiomycota (enzymologie)</term><term>Calcium (métabolisme)</term><term>Calcium (pharmacologie)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (enzymologie)</term><term>Escherichia coli (génétique)</term><term>Hème (métabolisme)</term><term>Hème (pharmacologie)</term><term>Isoenzymes (biosynthèse)</term><term>Isoenzymes (génétique)</term><term>Isoenzymes (métabolisme)</term><term>Peroxidases (biosynthèse)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Pliage des protéines (MeSH)</term><term>Protéines fongiques (biosynthèse)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Spectrophotométrie UV (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Fungal Proteins</term><term>Isoenzymes</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Complementary</term><term>Fungal Proteins</term><term>Isoenzymes</term><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium</term><term>Fungal Proteins</term><term>Heme</term><term>Isoenzymes</term><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Isoenzymes</term><term>Peroxidases</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN complémentaire</term><term>Escherichia coli</term><term>Isoenzymes</term><term>Peroxidases</term><term>Protéines fongiques</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Calcium</term><term>Hème</term><term>Isoenzymes</term><term>Peroxidases</term><term>Protéines fongiques</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Calcium</term><term>Hème</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Calcium</term><term>Heme</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Enzyme Activation</term><term>Molecular Sequence Data</term><term>Protein Folding</term><term>Spectrophotometry, Ultraviolet</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term><term>Données de séquences moléculaires</term><term>Pliage des protéines</term><term>Spectrophotométrie UV</term><term>Séquence nucléotidique</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">An engineered cDNA from Phanerochaete chrysosporium encoding both the mature and pro-sequence regions of Lip isoenzyme H8 (Lip) has been successfully overexpressed in Escherichia coli. The recombinant protein (LipP*) was sequestered in inclusion bodies. The reduced-denatured polypeptide has been purified by differential solubilization, and the active enzyme recovered after controlled in vitro refolding (albeit in low yield), by glutathione-mediated oxidation of disulphides, in a folding medium containing an intermediate concentration of urea, Ca2+, and haem. The procedure is analogous to that previously described for the production of active recombinant horseradish peroxidase (HRP-C*) from inclusion-body material. It is quite possible, therefore, that this type of procedure may be suitable for the recovery of most, if not all, active recombinant peroxidases. The resultant LipP* has spectral characteristics identical with that of the native enzyme as isolated from Phanerochaete chrysosporium. Its specific activity measured in the standard veratryl alcohol (VA) assay was 39 micromol of VA oxidized/min per mg of protein, a value which compares extremely favourably with that of the native enzyme (36 micromol of VA/min per mg). Although levels of active enzyme obtained are not yet as high as in the case of HRP-C* (1% conversion of crude inactive LipP* polypeptide into pure fully active Lip), it is envisaged that further refinement of the expression/folding/activation procedures will provide sufficient protein for biophysical characterization of both the wild-type and site-directed mutants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8670100</PMID><DateCompleted><Year>1996</Year><Month>08</Month><Day>05</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0264-6021</ISSN><JournalIssue CitedMedium="Print"><Volume>315 ( Pt 1)</Volume><PubDate><Year>1996</Year><Month>Apr</Month><Day>01</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Expression of lignin peroxidase H8 in Escherichia coli: folding and activation of the recombinant enzyme with Ca2+ and haem.</ArticleTitle><Pagination><MedlinePgn>15-9</MedlinePgn></Pagination><Abstract><AbstractText>An engineered cDNA from Phanerochaete chrysosporium encoding both the mature and pro-sequence regions of Lip isoenzyme H8 (Lip) has been successfully overexpressed in Escherichia coli. The recombinant protein (LipP*) was sequestered in inclusion bodies. The reduced-denatured polypeptide has been purified by differential solubilization, and the active enzyme recovered after controlled in vitro refolding (albeit in low yield), by glutathione-mediated oxidation of disulphides, in a folding medium containing an intermediate concentration of urea, Ca2+, and haem. The procedure is analogous to that previously described for the production of active recombinant horseradish peroxidase (HRP-C*) from inclusion-body material. It is quite possible, therefore, that this type of procedure may be suitable for the recovery of most, if not all, active recombinant peroxidases. The resultant LipP* has spectral characteristics identical with that of the native enzyme as isolated from Phanerochaete chrysosporium. Its specific activity measured in the standard veratryl alcohol (VA) assay was 39 micromol of VA oxidized/min per mg of protein, a value which compares extremely favourably with that of the native enzyme (36 micromol of VA/min per mg). Although levels of active enzyme obtained are not yet as high as in the case of HRP-C* (1% conversion of crude inactive LipP* polypeptide into pure fully active Lip), it is envisaged that further refinement of the expression/folding/activation procedures will provide sufficient protein for biophysical characterization of both the wild-type and site-directed mutants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Doyle</LastName><ForeName>W A</ForeName><Initials>WA</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, University of Sussex, Falmer, Brighton, U.K.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Smith</LastName><ForeName>A T</ForeName><Initials>AT</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, 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1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber><NameOfSubstance UI="D002118">Calcium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="Y">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013056" MajorTopicYN="N">Spectrophotometry, Ultraviolet</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year><Month>4</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1996</Year><Month>4</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1996</Year><Month>4</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8670100</ArticleId><ArticleId IdType="pmc">PMC1217164</ArticleId><ArticleId 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IdType="pubmed">7622486</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Sussex de l'Est</li></region><settlement><li>Brighton</li><li>Falmer</li></settlement><orgName><li>Université du Sussex</li></orgName></list><tree><noCountry><name sortKey="Smith, A T" sort="Smith, A T" uniqKey="Smith A" first="A T" last="Smith">A T Smith</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Doyle, W A" sort="Doyle, W A" uniqKey="Doyle W" first="W A" last="Doyle">W A Doyle</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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