[Exoproteinases of the oomycete Phytophthora infestans].
Identifieur interne : 002240 ( Main/Exploration ); précédent : 002239; suivant : 002241[Exoproteinases of the oomycete Phytophthora infestans].
Auteurs : E L Gvozdeva [Russie] ; E V Ievleva ; N G Gerasimova ; O L Ozeretskovskaia ; T A ValuevaSource :
- Prikladnaia biokhimiia i mikrobiologiia [ 0555-1099 ]
Descripteurs français
- KwdFr :
- Concentration en ions d'hydrogène (MeSH), Exopeptidases (composition chimique), Exopeptidases (métabolisme), Inhibiteurs de la sérine protéinase (métabolisme), Metalloproteases (analyse), Milieux de culture (MeSH), Phytophthora (croissance et développement), Phytophthora (enzymologie), Protéines végétales (métabolisme), Solanum tuberosum (métabolisme), Spécificité du substrat (MeSH), Subtilisine (analyse), Trypsine (analyse).
- MESH :
- analyse : Metalloproteases, Subtilisine, Trypsine.
- composition chimique : Exopeptidases.
- croissance et développement : Phytophthora.
- enzymologie : Phytophthora.
- métabolisme : Exopeptidases, Inhibiteurs de la sérine protéinase, Protéines végétales, Solanum tuberosum.
- Concentration en ions d'hydrogène, Milieux de culture, Spécificité du substrat.
English descriptors
- KwdEn :
- Culture Media (MeSH), Exopeptidases (chemistry), Exopeptidases (metabolism), Hydrogen-Ion Concentration (MeSH), Metalloproteases (analysis), Phytophthora (enzymology), Phytophthora (growth & development), Plant Proteins (metabolism), Serine Proteinase Inhibitors (metabolism), Solanum tuberosum (metabolism), Substrate Specificity (MeSH), Subtilisin (analysis), Trypsin (analysis).
- MESH :
- chemical , analysis : Metalloproteases, Subtilisin, Trypsin.
- chemical , chemistry : Exopeptidases.
- chemical , metabolism : Exopeptidases, Plant Proteins, Serine Proteinase Inhibitors.
- chemical : Culture Media.
- enzymology : Phytophthora.
- growth & development : Phytophthora.
- metabolism : Solanum tuberosum.
- Hydrogen-Ion Concentration, Substrate Specificity.
Abstract
When grown in a medium containing heat-stable potato tuber proteins, the oomycete Phytophthora infestans (Mont.) de Bary produces a set of exoproteinases active at neutral and mildly basic pH values. These extracellular proteinases have been shown by SDS-PAGE with the presence of gelatin to include at least six components differing in molecular weight. Inhibitory analysis and study of the effects of the enzymes on various synthetic substrates show that the culture liquid of P. infestans contains mainly serine proteinases specific to trypsin and subtilisin and metalloproteinases. Their activity is suppressed by proteinase-inhibitor proteins from potato tubers. It is suggested that P. infestans exoproteinases may be the metabolic target for natural proteinase inhibitors from potato.
PubMed: 15125197
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">[Exoproteinases of the oomycete Phytophthora infestans].</title><author><name sortKey="Gvozdeva, E L" sort="Gvozdeva, E L" uniqKey="Gvozdeva E" first="E L" last="Gvozdeva">E L Gvozdeva</name><affiliation wicri:level="3"><nlm:affiliation>Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 119071 Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Ievleva, E V" sort="Ievleva, E V" uniqKey="Ievleva E" first="E V" last="Ievleva">E V Ievleva</name></author><author><name sortKey="Gerasimova, N G" sort="Gerasimova, N G" uniqKey="Gerasimova N" first="N G" last="Gerasimova">N G Gerasimova</name></author><author><name sortKey="Ozeretskovskaia, O L" sort="Ozeretskovskaia, O L" uniqKey="Ozeretskovskaia O" first="O L" last="Ozeretskovskaia">O L Ozeretskovskaia</name></author><author><name sortKey="Valueva, T A" sort="Valueva, T A" uniqKey="Valueva T" first="T A" last="Valueva">T A Valueva</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004 Mar-Apr</date><idno type="RBID">pubmed:15125197</idno><idno type="pmid">15125197</idno><idno type="wicri:Area/Main/Corpus">002390</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002390</idno><idno type="wicri:Area/Main/Curation">002390</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002390</idno><idno type="wicri:Area/Main/Exploration">002390</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">[Exoproteinases of the oomycete Phytophthora infestans].</title><author><name sortKey="Gvozdeva, E L" sort="Gvozdeva, E L" uniqKey="Gvozdeva E" first="E L" last="Gvozdeva">E L Gvozdeva</name><affiliation wicri:level="3"><nlm:affiliation>Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 119071 Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Ievleva, E V" sort="Ievleva, E V" uniqKey="Ievleva E" first="E V" last="Ievleva">E V Ievleva</name></author><author><name sortKey="Gerasimova, N G" sort="Gerasimova, N G" uniqKey="Gerasimova N" first="N G" last="Gerasimova">N G Gerasimova</name></author><author><name sortKey="Ozeretskovskaia, O L" sort="Ozeretskovskaia, O L" uniqKey="Ozeretskovskaia O" first="O L" last="Ozeretskovskaia">O L Ozeretskovskaia</name></author><author><name sortKey="Valueva, T A" sort="Valueva, T A" uniqKey="Valueva T" first="T A" last="Valueva">T A Valueva</name></author></analytic><series><title level="j">Prikladnaia biokhimiia i mikrobiologiia</title><idno type="ISSN">0555-1099</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Culture Media (MeSH)</term><term>Exopeptidases (chemistry)</term><term>Exopeptidases (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Metalloproteases (analysis)</term><term>Phytophthora (enzymology)</term><term>Phytophthora (growth & development)</term><term>Plant Proteins (metabolism)</term><term>Serine Proteinase Inhibitors (metabolism)</term><term>Solanum tuberosum (metabolism)</term><term>Substrate Specificity (MeSH)</term><term>Subtilisin (analysis)</term><term>Trypsin (analysis)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Concentration en ions d'hydrogène (MeSH)</term><term>Exopeptidases (composition chimique)</term><term>Exopeptidases (métabolisme)</term><term>Inhibiteurs de la sérine protéinase (métabolisme)</term><term>Metalloproteases (analyse)</term><term>Milieux de culture (MeSH)</term><term>Phytophthora (croissance et développement)</term><term>Phytophthora (enzymologie)</term><term>Protéines végétales (métabolisme)</term><term>Solanum tuberosum (métabolisme)</term><term>Spécificité du substrat (MeSH)</term><term>Subtilisine (analyse)</term><term>Trypsine (analyse)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Metalloproteases</term><term>Subtilisin</term><term>Trypsin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Exopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Exopeptidases</term><term>Plant Proteins</term><term>Serine Proteinase Inhibitors</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Culture Media</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Metalloproteases</term><term>Subtilisine</term><term>Trypsine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Exopeptidases</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Phytophthora</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phytophthora</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phytophthora</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Phytophthora</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Exopeptidases</term><term>Inhibiteurs de la sérine protéinase</term><term>Protéines végétales</term><term>Solanum tuberosum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrogen-Ion Concentration</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Milieux de culture</term><term>Spécificité du substrat</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">When grown in a medium containing heat-stable potato tuber proteins, the oomycete Phytophthora infestans (Mont.) de Bary produces a set of exoproteinases active at neutral and mildly basic pH values. These extracellular proteinases have been shown by SDS-PAGE with the presence of gelatin to include at least six components differing in molecular weight. Inhibitory analysis and study of the effects of the enzymes on various synthetic substrates show that the culture liquid of P. infestans contains mainly serine proteinases specific to trypsin and subtilisin and metalloproteinases. Their activity is suppressed by proteinase-inhibitor proteins from potato tubers. It is suggested that P. infestans exoproteinases may be the metabolic target for natural proteinase inhibitors from potato.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15125197</PMID><DateCompleted><Year>2004</Year><Month>07</Month><Day>23</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0555-1099</ISSN><JournalIssue CitedMedium="Print"><Volume>40</Volume><Issue>2</Issue><PubDate><MedlineDate>2004 Mar-Apr</MedlineDate></PubDate></JournalIssue><Title>Prikladnaia biokhimiia i mikrobiologiia</Title><ISOAbbreviation>Prikl Biokhim Mikrobiol</ISOAbbreviation></Journal><ArticleTitle>[Exoproteinases of the oomycete Phytophthora infestans].</ArticleTitle><Pagination><MedlinePgn>194-200</MedlinePgn></Pagination><Abstract><AbstractText>When grown in a medium containing heat-stable potato tuber proteins, the oomycete Phytophthora infestans (Mont.) de Bary produces a set of exoproteinases active at neutral and mildly basic pH values. These extracellular proteinases have been shown by SDS-PAGE with the presence of gelatin to include at least six components differing in molecular weight. Inhibitory analysis and study of the effects of the enzymes on various synthetic substrates show that the culture liquid of P. infestans contains mainly serine proteinases specific to trypsin and subtilisin and metalloproteinases. Their activity is suppressed by proteinase-inhibitor proteins from potato tubers. It is suggested that P. infestans exoproteinases may be the metabolic target for natural proteinase inhibitors from potato.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gvozdeva</LastName><ForeName>E L</ForeName><Initials>EL</Initials><AffiliationInfo><Affiliation>Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 119071 Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ievleva</LastName><ForeName>E V</ForeName><Initials>EV</Initials></Author><Author ValidYN="Y"><LastName>Gerasimova</LastName><ForeName>N G</ForeName><Initials>NG</Initials></Author><Author ValidYN="Y"><LastName>Ozeretskovskaia</LastName><ForeName>O L</ForeName><Initials>OL</Initials></Author><Author ValidYN="Y"><LastName>Valueva</LastName><ForeName>T A</ForeName><Initials>TA</Initials></Author></AuthorList><Language>rus</Language><PublicationTypeList><PublicationType UI="D004740">English Abstract</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><VernacularTitle>Ekzoproteinazy oomitseta Phytophthora infestans.</VernacularTitle></Article><MedlineJournalInfo><Country>Russia (Federation)</Country><MedlineTA>Prikl Biokhim Mikrobiol</MedlineTA><NlmUniqueID>0023416</NlmUniqueID><ISSNLinking>0555-1099</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003470">Culture Media</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015842">Serine Proteinase Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D020689">Exopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D045726">Metalloproteases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber><NameOfSubstance UI="D014357">Trypsin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.62</RegistryNumber><NameOfSubstance UI="D020860">Subtilisin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003470" MajorTopicYN="N">Culture Media</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020689" MajorTopicYN="N">Exopeptidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045726" MajorTopicYN="N">Metalloproteases</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015842" MajorTopicYN="N">Serine Proteinase Inhibitors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011198" MajorTopicYN="N">Solanum tuberosum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020860" MajorTopicYN="N">Subtilisin</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014357" MajorTopicYN="N">Trypsin</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>5</Month><Day>6</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>7</Month><Day>24</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>5</Month><Day>6</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15125197</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Russie</li></country><region><li>District fédéral central</li></region><settlement><li>Moscou</li></settlement></list><tree><noCountry><name sortKey="Gerasimova, N G" sort="Gerasimova, N G" uniqKey="Gerasimova N" first="N G" last="Gerasimova">N G Gerasimova</name><name sortKey="Ievleva, E V" sort="Ievleva, E V" uniqKey="Ievleva E" first="E V" last="Ievleva">E V Ievleva</name><name sortKey="Ozeretskovskaia, O L" sort="Ozeretskovskaia, O L" uniqKey="Ozeretskovskaia O" first="O L" last="Ozeretskovskaia">O L Ozeretskovskaia</name><name sortKey="Valueva, T A" sort="Valueva, T A" uniqKey="Valueva T" first="T A" last="Valueva">T A Valueva</name></noCountry><country name="Russie"><region name="District fédéral central"><name sortKey="Gvozdeva, E L" sort="Gvozdeva, E L" uniqKey="Gvozdeva E" first="E L" last="Gvozdeva">E L Gvozdeva</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhytophthoraV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002240 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002240 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhytophthoraV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:15125197
|texte= [Exoproteinases of the oomycete Phytophthora infestans].
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:15125197" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhytophthoraV1
| This area was generated with Dilib version V0.6.38. |  |