Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium is synthesized as a preproenzyme.
Identifieur interne : 000F16 ( Main/Exploration ); précédent : 000F15; suivant : 000F17Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium is synthesized as a preproenzyme.
Auteurs : T G Ritch ; V J Nipper ; L. Akileswaran ; A J Smith ; D G Pribnow ; M H GoldSource :
- Gene [ 0378-1119 ] ; 1991.
Descripteurs français
- KwdFr :
- Basidiomycota (enzymologie), Basidiomycota (génétique), Biosynthèse des protéines (génétique), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Isoenzymes (génétique), Isoenzymes (métabolisme), Maturation post-traductionnelle des protéines (physiologie), Peroxidases (biosynthèse), Peroxidases (composition chimique), Peroxidases (génétique), Proenzymes (génétique), Proenzymes (métabolisme), Signaux de triage des protéines (génétique), Signaux de triage des protéines (métabolisme), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- biosynthèse : Peroxidases.
- composition chimique : Peroxidases.
- enzymologie : Basidiomycota.
- génétique : Basidiomycota, Biosynthèse des protéines, Isoenzymes, Peroxidases, Proenzymes, Signaux de triage des protéines.
- métabolisme : Isoenzymes, Proenzymes, Signaux de triage des protéines.
- physiologie : Maturation post-traductionnelle des protéines.
- Clonage moléculaire, Données de séquences moléculaires, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Basidiomycota (enzymology), Basidiomycota (genetics), Cloning, Molecular (MeSH), Enzyme Precursors (genetics), Enzyme Precursors (metabolism), Isoenzymes (genetics), Isoenzymes (metabolism), Molecular Sequence Data (MeSH), Peroxidases (biosynthesis), Peroxidases (chemistry), Peroxidases (genetics), Protein Biosynthesis (genetics), Protein Processing, Post-Translational (physiology), Protein Sorting Signals (genetics), Protein Sorting Signals (metabolism).
- MESH :
- chemical , biosynthesis : Peroxidases.
- chemical , chemistry : Peroxidases.
- chemical , genetics : Enzyme Precursors, Isoenzymes, Peroxidases, Protein Sorting Signals.
- enzymology : Basidiomycota.
- genetics : Basidiomycota, Protein Biosynthesis.
- chemical , metabolism : Enzyme Precursors, Isoenzymes, Protein Sorting Signals.
- physiology : Protein Processing, Post-Translational.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Molecular Sequence Data.
Abstract
The cDNA clone L18 encoding lignin peroxidase LiP2, the most highly expressed LiP isozyme from Phanerochaete chrysosporium strain OGC101, was isolated and sequenced. Comparison of the cDNA sequence with the N-terminal sequence of the mature LiP2 protein isolated from culture medium suggests that the mature protein contains 343 amino acids (aa) and is preceded by a 28-aa leader sequence. In vitro transcription followed by in vitro translation and processing by signal peptidase resulted in cleavage at a site following the Ala21 (counted from the N-terminal Met1 of the initial translation product). The resultant protein contains a 7-aa propeptide, indicating that LiP is synthesized as a preproenzyme.
DOI: 10.1016/0378-1119(91)90304-t
PubMed: 1743510
Affiliations:
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Akileswaran</name></author><author><name sortKey="Smith, A J" sort="Smith, A J" uniqKey="Smith A" first="A J" last="Smith">A J Smith</name></author><author><name sortKey="Pribnow, D G" sort="Pribnow, D G" uniqKey="Pribnow D" first="D G" last="Pribnow">D G Pribnow</name></author><author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></author></analytic><series><title level="j">Gene</title><idno type="ISSN">0378-1119</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>Basidiomycota (enzymology)</term><term>Basidiomycota (genetics)</term><term>Cloning, Molecular (MeSH)</term><term>Enzyme Precursors (genetics)</term><term>Enzyme Precursors (metabolism)</term><term>Isoenzymes (genetics)</term><term>Isoenzymes (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Peroxidases (biosynthesis)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (genetics)</term><term>Protein Biosynthesis (genetics)</term><term>Protein Processing, Post-Translational (physiology)</term><term>Protein Sorting Signals (genetics)</term><term>Protein Sorting Signals (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (enzymologie)</term><term>Basidiomycota (génétique)</term><term>Biosynthèse des protéines (génétique)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Isoenzymes (génétique)</term><term>Isoenzymes (métabolisme)</term><term>Maturation post-traductionnelle des protéines (physiologie)</term><term>Peroxidases (biosynthèse)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (génétique)</term><term>Proenzymes (génétique)</term><term>Proenzymes (métabolisme)</term><term>Signaux de triage des protéines (génétique)</term><term>Signaux de triage des protéines (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Enzyme Precursors</term><term>Isoenzymes</term><term>Peroxidases</term><term>Protein Sorting Signals</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Basidiomycota</term><term>Protein Biosynthesis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Basidiomycota</term><term>Biosynthèse des protéines</term><term>Isoenzymes</term><term>Peroxidases</term><term>Proenzymes</term><term>Signaux de triage des protéines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Enzyme Precursors</term><term>Isoenzymes</term><term>Protein Sorting Signals</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Isoenzymes</term><term>Proenzymes</term><term>Signaux de triage des protéines</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Maturation post-traductionnelle des protéines</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protein Processing, Post-Translational</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Molecular Sequence Data</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The cDNA clone L18 encoding lignin peroxidase LiP2, the most highly expressed LiP isozyme from Phanerochaete chrysosporium strain OGC101, was isolated and sequenced. Comparison of the cDNA sequence with the N-terminal sequence of the mature LiP2 protein isolated from culture medium suggests that the mature protein contains 343 amino acids (aa) and is preceded by a 28-aa leader sequence. In vitro transcription followed by in vitro translation and processing by signal peptidase resulted in cleavage at a site following the Ala21 (counted from the N-terminal Met1 of the initial translation product). The resultant protein contains a 7-aa propeptide, indicating that LiP is synthesized as a preproenzyme.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1743510</PMID><DateCompleted><Year>1992</Year><Month>01</Month><Day>13</Day></DateCompleted><DateRevised><Year>2019</Year><Month>07</Month><Day>07</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0378-1119</ISSN><JournalIssue CitedMedium="Print"><Volume>107</Volume><Issue>1</Issue><PubDate><Year>1991</Year><Month>Oct</Month><Day>30</Day></PubDate></JournalIssue><Title>Gene</Title><ISOAbbreviation>Gene</ISOAbbreviation></Journal><ArticleTitle>Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium is synthesized as a preproenzyme.</ArticleTitle><Pagination><MedlinePgn>119-26</MedlinePgn></Pagination><Abstract><AbstractText>The cDNA clone L18 encoding lignin peroxidase LiP2, the most highly expressed LiP isozyme from Phanerochaete chrysosporium strain OGC101, was isolated and sequenced. Comparison of the cDNA sequence with the N-terminal sequence of the mature LiP2 protein isolated from culture medium suggests that the mature protein contains 343 amino acids (aa) and is preceded by a 28-aa leader sequence. In vitro transcription followed by in vitro translation and processing by signal peptidase resulted in cleavage at a site following the Ala21 (counted from the N-terminal Met1 of the initial translation product). The resultant protein contains a 7-aa propeptide, indicating that LiP is synthesized as a preproenzyme.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ritch</LastName><ForeName>T G</ForeName><Initials>TG</Initials><Suffix>Jr</Suffix><AffiliationInfo><Affiliation>Department of Chemical and Biological Sciences, Oregon Graduate Institute for Science and Technology, Beaverton 97006-1999.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nipper</LastName><ForeName>V J</ForeName><Initials>VJ</Initials></Author><Author ValidYN="Y"><LastName>Akileswaran</LastName><ForeName>L</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Smith</LastName><ForeName>A J</ForeName><Initials>AJ</Initials></Author><Author ValidYN="Y"><LastName>Pribnow</LastName><ForeName>D G</ForeName><Initials>DG</Initials></Author><Author ValidYN="Y"><LastName>Gold</LastName><ForeName>M 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MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">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="Y">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014176" MajorTopicYN="N">Protein Biosynthesis</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021382" MajorTopicYN="N">Protein Sorting Signals</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>11</Month><Day>9</Day><Hour>19</Hour><Minute>15</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>3</Month><Day>28</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>11</Month><Day>9</Day><Hour>19</Hour><Minute>15</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1743510</ArticleId><ArticleId IdType="pii">0378-1119(91)90304-T</ArticleId><ArticleId IdType="doi">10.1016/0378-1119(91)90304-t</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Akileswaran, L" sort="Akileswaran, L" uniqKey="Akileswaran L" first="L" last="Akileswaran">L. Akileswaran</name><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name><name sortKey="Nipper, V J" sort="Nipper, V J" uniqKey="Nipper V" first="V J" last="Nipper">V J Nipper</name><name sortKey="Pribnow, D G" sort="Pribnow, D G" uniqKey="Pribnow D" first="D G" last="Pribnow">D G Pribnow</name><name sortKey="Ritch, T G" sort="Ritch, T G" uniqKey="Ritch T" first="T G" last="Ritch">T G Ritch</name><name sortKey="Smith, A J" sort="Smith, A J" uniqKey="Smith A" first="A J" last="Smith">A J Smith</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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