Links to Exploration step
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific γ-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)</title><author><name sortKey="Grill, Erwin" sort="Grill, Erwin" uniqKey="Grill E" first="Erwin" last="Grill">Erwin Grill</name><affiliation><nlm:aff id="af1">Lehrstuhl für Pharmazeutische Biologie, Universität München, Karlstrasse 29, D-8000 München 2, Federal Republic of Germany</nlm:aff></affiliation></author><author><name sortKey="Loffler, Susanne" sort="Loffler, Susanne" uniqKey="Loffler S" first="Susanne" last="Löffler">Susanne Löffler</name><affiliation><nlm:aff id="af1">Lehrstuhl für Pharmazeutische Biologie, Universität München, Karlstrasse 29, D-8000 München 2, Federal Republic of Germany</nlm:aff></affiliation></author><author><name sortKey="Winnacker, Ernst L" sort="Winnacker, Ernst L" uniqKey="Winnacker E" first="Ernst-L." last="Winnacker">Ernst-L. Winnacker</name><affiliation><nlm:aff id="af2">Genzentrum der Universität München, Am Klopferspitz, D-8033 Martinsried, Federal Republic of Germany</nlm:aff></affiliation></author><author><name sortKey="Zenk, Meinhart H" sort="Zenk, Meinhart H" uniqKey="Zenk M" first="Meinhart H." last="Zenk">Meinhart H. Zenk</name><affiliation><nlm:aff id="af1">Lehrstuhl für Pharmazeutische Biologie, Universität München, Karlstrasse 29, D-8000 München 2, Federal Republic of Germany</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">16594069</idno><idno type="pmc">297945</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC297945</idno><idno type="RBID">PMC:297945</idno><date when="1989">1989</date><idno type="wicri:Area/Pmc/Corpus">000105</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000105</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific γ-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)</title><author><name sortKey="Grill, Erwin" sort="Grill, Erwin" uniqKey="Grill E" first="Erwin" last="Grill">Erwin Grill</name><affiliation><nlm:aff id="af1">Lehrstuhl für Pharmazeutische Biologie, Universität München, Karlstrasse 29, D-8000 München 2, Federal Republic of Germany</nlm:aff></affiliation></author><author><name sortKey="Loffler, Susanne" sort="Loffler, Susanne" uniqKey="Loffler S" first="Susanne" last="Löffler">Susanne Löffler</name><affiliation><nlm:aff id="af1">Lehrstuhl für Pharmazeutische Biologie, Universität München, Karlstrasse 29, D-8000 München 2, Federal Republic of Germany</nlm:aff></affiliation></author><author><name sortKey="Winnacker, Ernst L" sort="Winnacker, Ernst L" uniqKey="Winnacker E" first="Ernst-L." last="Winnacker">Ernst-L. Winnacker</name><affiliation><nlm:aff id="af2">Genzentrum der Universität München, Am Klopferspitz, D-8033 Martinsried, Federal Republic of Germany</nlm:aff></affiliation></author><author><name sortKey="Zenk, Meinhart H" sort="Zenk, Meinhart H" uniqKey="Zenk M" first="Meinhart H." last="Zenk">Meinhart H. Zenk</name><affiliation><nlm:aff id="af1">Lehrstuhl für Pharmazeutische Biologie, Universität München, Karlstrasse 29, D-8000 München 2, Federal Republic of Germany</nlm:aff></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="1989">1989</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>An enzyme has been discovered and characterized from <italic>Silene cucubalus</italic> cell suspension cultures that catalyzes the transfer of the γ-glutamylcysteine dipeptide moiety of glutathione to an acceptor glutathione molecule or a growing chain of [Glu(-Cys)]<italic><sub>n</sub></italic>-Gly oligomers, thus synthesizing phytochelatins, the metal-binding peptides of higher plants and select fungi. The enzyme was named γ-glutamylcysteine dipeptidyl transpeptidase and given the trivial name phytochelatin synthase. The primary reaction catalyzed is [Glu(-Cys)]-Gly + [Glu(-Cys)]<italic><sub>n</sub></italic>-Gly → [Glu(-Cys)]<sub><italic>n</italic>+1</sub>-Gly + Gly. The enzyme is isoelectric near pH 4.8 and has temperature and pH optima at 35°C and 7.9, respectively. Phytochelatin synthase is constitutively present in cell cultures of various plant species and its formation is not noticeably induced by heavy metal ions in the growth medium. The enzyme (<italic>M</italic><sub>r</sub>95,000) seems to be composed of four subunits, the dimer (<italic>M</italic><sub>r</sub>50,000) being also catalytically active. Cd<sup>2+</sup> is by far the best metal activator of the enzyme followed by Ag<sup>+</sup>, Bi<sup>3+</sup>, Pb<sup>2+</sup>, Zn<sup>2+</sup>, Cu<sup>2+</sup>, Hg<sup>2+</sup>, and Au<sup>+</sup>. The <italic>K</italic><sub>m</sub> for glutathione is 6.7 mM. The enzyme activity seems to be self-regulated in that the product of the reaction (the phytochelatins) chelates the enzyme-activating metal, thus terminating the enzyme reaction. The molar ratio of the γ-glutamylcysteine dipeptide in phytochelatin to Cd<sup>2+</sup> in the newly formed complex was 2:1.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Proc Natl Acad Sci U S A</journal-id><journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title><issn pub-type="ppub">0027-8424</issn><issn pub-type="epub">1091-6490</issn></journal-meta><article-meta><article-id pub-id-type="pmid">16594069</article-id><article-id pub-id-type="pmc">297945</article-id><article-categories><subj-group subj-group-type="heading"><subject>Biological Sciences: Biochemistry</subject></subj-group></article-categories><title-group><article-title>Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific γ-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Grill</surname><given-names>Erwin</given-names></name><xref ref-type="aff" rid="af1">*</xref></contrib><contrib contrib-type="author"><name><surname>Löffler</surname><given-names>Susanne</given-names></name><xref ref-type="aff" rid="af1">*</xref></contrib><contrib contrib-type="author"><name><surname>Winnacker</surname><given-names>Ernst-L.</given-names></name><xref ref-type="aff" rid="af2">†</xref></contrib><contrib contrib-type="author"><name><surname>Zenk</surname><given-names>Meinhart H.</given-names></name><xref ref-type="aff" rid="af1">*</xref></contrib></contrib-group><aff id="af1"><label>*</label>Lehrstuhl für Pharmazeutische Biologie, Universität München, Karlstrasse 29, D-8000 München 2, Federal Republic of Germany</aff><aff id="af2"><label>†</label>Genzentrum der Universität München, Am Klopferspitz, D-8033 Martinsried, Federal Republic of Germany</aff><pub-date pub-type="ppub"><month>09</month><year>1989</year></pub-date><volume>86</volume><issue>18</issue><fpage>6838</fpage><lpage>6842</lpage><abstract><p>An enzyme has been discovered and characterized from <italic>Silene cucubalus</italic> cell suspension cultures that catalyzes the transfer of the γ-glutamylcysteine dipeptide moiety of glutathione to an acceptor glutathione molecule or a growing chain of [Glu(-Cys)]<italic><sub>n</sub></italic>-Gly oligomers, thus synthesizing phytochelatins, the metal-binding peptides of higher plants and select fungi. The enzyme was named γ-glutamylcysteine dipeptidyl transpeptidase and given the trivial name phytochelatin synthase. The primary reaction catalyzed is [Glu(-Cys)]-Gly + [Glu(-Cys)]<italic><sub>n</sub></italic>-Gly → [Glu(-Cys)]<sub><italic>n</italic>+1</sub>-Gly + Gly. The enzyme is isoelectric near pH 4.8 and has temperature and pH optima at 35°C and 7.9, respectively. Phytochelatin synthase is constitutively present in cell cultures of various plant species and its formation is not noticeably induced by heavy metal ions in the growth medium. The enzyme (<italic>M</italic><sub>r</sub>95,000) seems to be composed of four subunits, the dimer (<italic>M</italic><sub>r</sub>50,000) being also catalytically active. Cd<sup>2+</sup> is by far the best metal activator of the enzyme followed by Ag<sup>+</sup>, Bi<sup>3+</sup>, Pb<sup>2+</sup>, Zn<sup>2+</sup>, Cu<sup>2+</sup>, Hg<sup>2+</sup>, and Au<sup>+</sup>. The <italic>K</italic><sub>m</sub> for glutathione is 6.7 mM. The enzyme activity seems to be self-regulated in that the product of the reaction (the phytochelatins) chelates the enzyme-activating metal, thus terminating the enzyme reaction. The molar ratio of the γ-glutamylcysteine dipeptide in phytochelatin to Cd<sup>2+</sup> in the newly formed complex was 2:1.</p></abstract><kwd-group><kwd>detoxification</kwd><kwd>dipeptidyl transpeptidase</kwd><kwd>phytochelatin biosynthesis</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Linguistique/explor/TamazightV2/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 0001059 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 0001059 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Linguistique
|area= TamazightV2
|flux= Pmc
|étape= Corpus
|type= RBID
|clé=
|texte=
}}
| This area was generated with Dilib version V0.6.33. |  |