Complete amino acid sequence of plastocyanin from a green alga, Enteromorpha prolifera.
Identifieur interne : 004D88 ( Main/Exploration ); précédent : 004D87; suivant : 004D89Complete amino acid sequence of plastocyanin from a green alga, Enteromorpha prolifera.
Auteurs : R J Simpson ; R L Moritz ; E C Nice ; B. Grego ; F. Yoshizaki ; Y. Sugimura ; H C Freeman ; M. MurataSource :
- European journal of biochemistry [ 0014-2956 ] ; 1986.
Descripteurs français
- KwdFr :
- Carboxypeptidases (MeSH), Chlorophyta (analyse), Chromatographie en phase liquide à haute performance (MeSH), Chymotrypsine (MeSH), Endopeptidases (MeSH), Fragments peptidiques (MeSH), Metalloendopeptidases (MeSH), Plastocyanine (MeSH), Protéines végétales (MeSH), Serine endopeptidases (MeSH), Séquence d'acides aminés (MeSH), Trypsine (MeSH).
- MESH :
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Carboxypeptidases (MeSH), Chlorophyta (analysis), Chromatography, High Pressure Liquid (MeSH), Chymotrypsin (MeSH), Endopeptidases (MeSH), Metalloendopeptidases (MeSH), Peptide Fragments (MeSH), Plant Proteins (MeSH), Plastocyanin (MeSH), Serine Endopeptidases (MeSH), Trypsin (MeSH).
- MESH :
Abstract
The complete amino acid sequence of the plastocyanin from the green alga Enteromorpha prolifera has been determined by Edman degradation of the intact molecule and fragments produced by enzymatic cleavage of the polypeptide chain with chymotrypsin, Staphylococcus aureus protease, proline-specific endopeptidase, Lys-C endopeptidase and trypsin. The molecule consists of 98 amino acid residues with a calculated relative molecular mass of 10103. The amino acid sequence of E. prolifera plastocyanin shows a high degree of homology with those plastocyanins from other algae and higher plants. In particular, the four residues which are copper ligands in other plastocyanins and in the bacterial electron transport protein azurin (two histidines, one cysteine and one methionine) are conserved. Five out of the six acidic amino acid side-chains which create an 'acidic patch' on the surface of plastocyanin from Populus nigra var. italica [Colman, P. M. et al. (1978) Nature (Lond.) 272, 319-324] are conserved in the amino acid sequence of E. prolifera plastocyanin.
DOI: 10.1111/j.1432-1033.1986.tb09694.x
PubMed: 3522227
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Complete amino acid sequence of plastocyanin from a green alga, Enteromorpha prolifera.</title><author><name sortKey="Simpson, R J" sort="Simpson, R J" uniqKey="Simpson R" first="R J" last="Simpson">R J Simpson</name></author><author><name sortKey="Moritz, R L" sort="Moritz, R L" uniqKey="Moritz R" first="R L" last="Moritz">R L Moritz</name></author><author><name sortKey="Nice, E C" sort="Nice, E C" uniqKey="Nice E" first="E C" last="Nice">E C Nice</name></author><author><name sortKey="Grego, B" sort="Grego, B" uniqKey="Grego B" first="B" last="Grego">B. Grego</name></author><author><name sortKey="Yoshizaki, F" sort="Yoshizaki, F" uniqKey="Yoshizaki F" first="F" last="Yoshizaki">F. Yoshizaki</name></author><author><name sortKey="Sugimura, Y" sort="Sugimura, Y" uniqKey="Sugimura Y" first="Y" last="Sugimura">Y. Sugimura</name></author><author><name sortKey="Freeman, H C" sort="Freeman, H C" uniqKey="Freeman H" first="H C" last="Freeman">H C Freeman</name></author><author><name sortKey="Murata, M" sort="Murata, M" uniqKey="Murata M" first="M" last="Murata">M. Murata</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1986">1986</date><idno type="RBID">pubmed:3522227</idno><idno type="pmid">3522227</idno><idno type="doi">10.1111/j.1432-1033.1986.tb09694.x</idno><idno type="wicri:Area/Main/Corpus">004D82</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004D82</idno><idno type="wicri:Area/Main/Curation">004D82</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004D82</idno><idno type="wicri:Area/Main/Exploration">004D82</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Complete amino acid sequence of plastocyanin from a green alga, Enteromorpha prolifera.</title><author><name sortKey="Simpson, R J" sort="Simpson, R J" uniqKey="Simpson R" first="R J" last="Simpson">R J Simpson</name></author><author><name sortKey="Moritz, R L" sort="Moritz, R L" uniqKey="Moritz R" first="R L" last="Moritz">R L Moritz</name></author><author><name sortKey="Nice, E C" sort="Nice, E C" uniqKey="Nice E" first="E C" last="Nice">E C Nice</name></author><author><name sortKey="Grego, B" sort="Grego, B" uniqKey="Grego B" first="B" last="Grego">B. Grego</name></author><author><name sortKey="Yoshizaki, F" sort="Yoshizaki, F" uniqKey="Yoshizaki F" first="F" last="Yoshizaki">F. Yoshizaki</name></author><author><name sortKey="Sugimura, Y" sort="Sugimura, Y" uniqKey="Sugimura Y" first="Y" last="Sugimura">Y. Sugimura</name></author><author><name sortKey="Freeman, H C" sort="Freeman, H C" uniqKey="Freeman H" first="H C" last="Freeman">H C Freeman</name></author><author><name sortKey="Murata, M" sort="Murata, M" uniqKey="Murata M" first="M" last="Murata">M. Murata</name></author></analytic><series><title level="j">European journal of biochemistry</title><idno type="ISSN">0014-2956</idno><imprint><date when="1986" type="published">1986</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Carboxypeptidases (MeSH)</term><term>Chlorophyta (analysis)</term><term>Chromatography, High Pressure Liquid (MeSH)</term><term>Chymotrypsin (MeSH)</term><term>Endopeptidases (MeSH)</term><term>Metalloendopeptidases (MeSH)</term><term>Peptide Fragments (MeSH)</term><term>Plant Proteins (MeSH)</term><term>Plastocyanin (MeSH)</term><term>Serine Endopeptidases (MeSH)</term><term>Trypsin (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Carboxypeptidases (MeSH)</term><term>Chlorophyta (analyse)</term><term>Chromatographie en phase liquide à haute performance (MeSH)</term><term>Chymotrypsine (MeSH)</term><term>Endopeptidases (MeSH)</term><term>Fragments peptidiques (MeSH)</term><term>Metalloendopeptidases (MeSH)</term><term>Plastocyanine (MeSH)</term><term>Protéines végétales (MeSH)</term><term>Serine endopeptidases (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Trypsine (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Carboxypeptidases</term><term>Chymotrypsin</term><term>Endopeptidases</term><term>Metalloendopeptidases</term><term>Peptide Fragments</term><term>Plant Proteins</term><term>Plastocyanin</term><term>Serine Endopeptidases</term><term>Trypsin</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Chlorophyta</term></keywords><keywords scheme="MESH" qualifier="analysis" xml:lang="en"><term>Chlorophyta</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Chromatography, High Pressure Liquid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Carboxypeptidases</term><term>Chromatographie en phase liquide à haute performance</term><term>Chymotrypsine</term><term>Endopeptidases</term><term>Fragments peptidiques</term><term>Metalloendopeptidases</term><term>Plastocyanine</term><term>Protéines végétales</term><term>Serine endopeptidases</term><term>Séquence d'acides aminés</term><term>Trypsine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The complete amino acid sequence of the plastocyanin from the green alga Enteromorpha prolifera has been determined by Edman degradation of the intact molecule and fragments produced by enzymatic cleavage of the polypeptide chain with chymotrypsin, Staphylococcus aureus protease, proline-specific endopeptidase, Lys-C endopeptidase and trypsin. The molecule consists of 98 amino acid residues with a calculated relative molecular mass of 10103. The amino acid sequence of E. prolifera plastocyanin shows a high degree of homology with those plastocyanins from other algae and higher plants. In particular, the four residues which are copper ligands in other plastocyanins and in the bacterial electron transport protein azurin (two histidines, one cysteine and one methionine) are conserved. Five out of the six acidic amino acid side-chains which create an 'acidic patch' on the surface of plastocyanin from Populus nigra var. italica [Colman, P. M. et al. (1978) Nature (Lond.) 272, 319-324] are conserved in the amino acid sequence of E. prolifera plastocyanin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">3522227</PMID><DateCompleted><Year>1986</Year><Month>08</Month><Day>20</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-2956</ISSN><JournalIssue CitedMedium="Print"><Volume>157</Volume><Issue>3</Issue><PubDate><Year>1986</Year><Month>Jun</Month><Day>16</Day></PubDate></JournalIssue><Title>European journal of biochemistry</Title><ISOAbbreviation>Eur J Biochem</ISOAbbreviation></Journal><ArticleTitle>Complete amino acid sequence of plastocyanin from a green alga, Enteromorpha prolifera.</ArticleTitle><Pagination><MedlinePgn>497-506</MedlinePgn></Pagination><Abstract><AbstractText>The complete amino acid sequence of the plastocyanin from the green alga Enteromorpha prolifera has been determined by Edman degradation of the intact molecule and fragments produced by enzymatic cleavage of the polypeptide chain with chymotrypsin, Staphylococcus aureus protease, proline-specific endopeptidase, Lys-C endopeptidase and trypsin. The molecule consists of 98 amino acid residues with a calculated relative molecular mass of 10103. The amino acid sequence of E. prolifera plastocyanin shows a high degree of homology with those plastocyanins from other algae and higher plants. In particular, the four residues which are copper ligands in other plastocyanins and in the bacterial electron transport protein azurin (two histidines, one cysteine and one methionine) are conserved. Five out of the six acidic amino acid side-chains which create an 'acidic patch' on the surface of plastocyanin from Populus nigra var. italica [Colman, P. M. et al. (1978) Nature (Lond.) 272, 319-324] are conserved in the amino acid sequence of E. prolifera plastocyanin.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Simpson</LastName><ForeName>R J</ForeName><Initials>RJ</Initials></Author><Author ValidYN="Y"><LastName>Moritz</LastName><ForeName>R L</ForeName><Initials>RL</Initials></Author><Author ValidYN="Y"><LastName>Nice</LastName><ForeName>E C</ForeName><Initials>EC</Initials></Author><Author ValidYN="Y"><LastName>Grego</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Yoshizaki</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Sugimura</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Freeman</LastName><ForeName>H C</ForeName><Initials>HC</Initials></Author><Author ValidYN="Y"><LastName>Murata</LastName><ForeName>M</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Eur J Biochem</MedlineTA><NlmUniqueID>0107600</NlmUniqueID><ISSNLinking>0014-2956</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9014-09-9</RegistryNumber><NameOfSubstance UI="D010970">Plastocyanin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D002268">Carboxypeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010450">Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.16.5</RegistryNumber><NameOfSubstance UI="C022633">serine carboxypeptidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="D012697">Serine Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.1</RegistryNumber><NameOfSubstance UI="D002918">Chymotrypsin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.26</RegistryNumber><NameOfSubstance UI="C022432">prolyl oligopeptidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber><NameOfSubstance UI="D014357">Trypsin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.50</RegistryNumber><NameOfSubstance UI="C036813">lysyl endopeptidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.-</RegistryNumber><NameOfSubstance UI="D008666">Metalloendopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.29</RegistryNumber><NameOfSubstance UI="C022653">auR protein, Staphylococcus aureus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002268" MajorTopicYN="N">Carboxypeptidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000460" MajorTopicYN="N">Chlorophyta</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002918" MajorTopicYN="N">Chymotrypsin</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010450" MajorTopicYN="N">Endopeptidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008666" MajorTopicYN="Y">Metalloendopeptidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="Y">Plant Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010970" MajorTopicYN="Y">Plastocyanin</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012697" MajorTopicYN="Y">Serine Endopeptidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014357" MajorTopicYN="N">Trypsin</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1986</Year><Month>6</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1986</Year><Month>6</Month><Day>16</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1986</Year><Month>6</Month><Day>16</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">3522227</ArticleId><ArticleId IdType="doi">10.1111/j.1432-1033.1986.tb09694.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Freeman, H C" sort="Freeman, H C" uniqKey="Freeman H" first="H C" last="Freeman">H C Freeman</name><name sortKey="Grego, B" sort="Grego, B" uniqKey="Grego B" first="B" last="Grego">B. Grego</name><name sortKey="Moritz, R L" sort="Moritz, R L" uniqKey="Moritz R" first="R L" last="Moritz">R L Moritz</name><name sortKey="Murata, M" sort="Murata, M" uniqKey="Murata M" first="M" last="Murata">M. Murata</name><name sortKey="Nice, E C" sort="Nice, E C" uniqKey="Nice E" first="E C" last="Nice">E C Nice</name><name sortKey="Simpson, R J" sort="Simpson, R J" uniqKey="Simpson R" first="R J" last="Simpson">R J Simpson</name><name sortKey="Sugimura, Y" sort="Sugimura, Y" uniqKey="Sugimura Y" first="Y" last="Sugimura">Y. Sugimura</name><name sortKey="Yoshizaki, F" sort="Yoshizaki, F" uniqKey="Yoshizaki F" first="F" last="Yoshizaki">F. Yoshizaki</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PoplarV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 004D88 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 004D88 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PoplarV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:3522227
|texte= Complete amino acid sequence of plastocyanin from a green alga, Enteromorpha prolifera.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:3522227" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PoplarV1
| This area was generated with Dilib version V0.6.37. |  |