Expression of the lignin peroxidase H2 gene from Phanerochaete chrysosporium in Escherichia coli.
Identifieur interne : 000B75 ( Main/Exploration ); précédent : 000B74; suivant : 000B76Expression of the lignin peroxidase H2 gene from Phanerochaete chrysosporium in Escherichia coli.
Auteurs : G. Nie [États-Unis] ; N S Reading ; S D AustSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1998.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , biosynthesis : Peroxidases.
- genetics : Escherichia coli, Fungi, Peroxidases.
- Gene Expression Regulation, Bacterial, Gene Expression Regulation, Fungal, Genes, Fungal.
Abstract
The DNA sequence for the extracellular lignin peroxidase isozyme H2 from Phanerochaete chrysosporium, obtained from cDNA clone lambda ML-6, was synthesized by PCR and successfully expressed in Escherichia coli under control of the T7 promoter. The portion of the cDNA encoding the signal peptide, not found in the mature native enzyme, was not included. Recombinated lignin peroxidase H2 (rLiPH2) was produced in inclusion bodies in an inactive form. Active enzyme was obtained by refolding with glutathione-mediated oxidation in a medium containing urea, Ca2+, and hemin. The recombinant enzyme had spectral characteristics and kinetic properties identical to that of native enzyme isolated from P. chrysosporium. Surprisingly, rLiPH2, like the native enzyme, also exhibited some manganese peroxidase activity.
DOI: 10.1006/bbrc.1998.9106
PubMed: 9705846
Affiliations:
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Le document en format XML
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Nie</name><affiliation wicri:level="1"><nlm:affiliation>Biotechnology Center, Utah State University, Logan 84322-4705, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biotechnology Center, Utah State University, Logan 84322-4705</wicri:regionArea><wicri:noRegion>Logan 84322-4705</wicri:noRegion></affiliation></author><author><name sortKey="Reading, N S" sort="Reading, N S" uniqKey="Reading N" first="N S" last="Reading">N S Reading</name></author><author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Escherichia coli (genetics)</term><term>Fungi (genetics)</term><term>Gene Expression Regulation, Bacterial (MeSH)</term><term>Gene Expression Regulation, Fungal (MeSH)</term><term>Genes, Fungal (MeSH)</term><term>Peroxidases (biosynthesis)</term><term>Peroxidases (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Champignons (génétique)</term><term>Escherichia coli (génétique)</term><term>Gènes fongiques (MeSH)</term><term>Peroxidases (biosynthèse)</term><term>Peroxidases (génétique)</term><term>Régulation de l'expression des gènes bactériens (MeSH)</term><term>Régulation de l'expression des gènes fongiques (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term><term>Fungi</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Champignons</term><term>Escherichia coli</term><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Expression Regulation, Bacterial</term><term>Gene Expression Regulation, Fungal</term><term>Genes, Fungal</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Gènes fongiques</term><term>Régulation de l'expression des gènes bactériens</term><term>Régulation de l'expression des gènes fongiques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The DNA sequence for the extracellular lignin peroxidase isozyme H2 from Phanerochaete chrysosporium, obtained from cDNA clone lambda ML-6, was synthesized by PCR and successfully expressed in Escherichia coli under control of the T7 promoter. The portion of the cDNA encoding the signal peptide, not found in the mature native enzyme, was not included. Recombinated lignin peroxidase H2 (rLiPH2) was produced in inclusion bodies in an inactive form. Active enzyme was obtained by refolding with glutathione-mediated oxidation in a medium containing urea, Ca2+, and hemin. The recombinant enzyme had spectral characteristics and kinetic properties identical to that of native enzyme isolated from P. chrysosporium. Surprisingly, rLiPH2, like the native enzyme, also exhibited some manganese peroxidase activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9705846</PMID><DateCompleted><Year>1998</Year><Month>09</Month><Day>17</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>249</Volume><Issue>1</Issue><PubDate><Year>1998</Year><Month>Aug</Month><Day>10</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Expression of the lignin peroxidase H2 gene from Phanerochaete chrysosporium in Escherichia coli.</ArticleTitle><Pagination><MedlinePgn>146-50</MedlinePgn></Pagination><Abstract><AbstractText>The DNA sequence for the extracellular lignin peroxidase isozyme H2 from Phanerochaete chrysosporium, obtained from cDNA clone lambda ML-6, was synthesized by PCR and successfully expressed in Escherichia coli under control of the T7 promoter. The portion of the cDNA encoding the signal peptide, not found in the mature native enzyme, was not included. Recombinated lignin peroxidase H2 (rLiPH2) was produced in inclusion bodies in an inactive form. Active enzyme was obtained by refolding with glutathione-mediated oxidation in a medium containing urea, Ca2+, and hemin. The recombinant enzyme had spectral characteristics and kinetic properties identical to that of native enzyme isolated from P. chrysosporium. 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