Specific protein regions influence substrate specificity and product length in polyunsaturated fatty acid condensing enzymes.
Identifieur interne : 001834 ( Main/Exploration ); précédent : 001833; suivant : 001835Specific protein regions influence substrate specificity and product length in polyunsaturated fatty acid condensing enzymes.
Auteurs : Patricia L. Vrinten [Canada] ; Travis Hoffman ; Jörg Bauer ; Xiao QiuSource :
- Biochemistry [ 1520-4995 ] ; 2010.
Descripteurs français
- KwdFr :
- Acetyltransferases (composition chimique), Acetyltransferases (génétique), Acetyltransferases (isolement et purification), Acetyltransferases (métabolisme), Acides gras insaturés (composition chimique), Acides gras insaturés (métabolisme), Motifs d'acides aminés (MeSH), Protéines d'algue (composition chimique), Protéines d'algue (génétique), Protéines d'algue (isolement et purification), Protéines d'algue (métabolisme), Pythium (composition chimique), Pythium (enzymologie), Pythium (génétique), Spécificité du substrat (MeSH).
- MESH :
- composition chimique : Acetyltransferases, Acides gras insaturés, Protéines d'algue, Pythium.
- enzymologie : Pythium.
- génétique : Acetyltransferases, Protéines d'algue, Pythium.
- isolement et purification : Acetyltransferases, Protéines d'algue.
- métabolisme : Acetyltransferases, Acides gras insaturés, Protéines d'algue.
- Motifs d'acides aminés, Spécificité du substrat.
English descriptors
- KwdEn :
- Acetyltransferases (chemistry), Acetyltransferases (genetics), Acetyltransferases (isolation & purification), Acetyltransferases (metabolism), Algal Proteins (chemistry), Algal Proteins (genetics), Algal Proteins (isolation & purification), Algal Proteins (metabolism), Amino Acid Motifs (MeSH), Fatty Acid Elongases (MeSH), Fatty Acids, Unsaturated (chemistry), Fatty Acids, Unsaturated (metabolism), Pythium (chemistry), Pythium (enzymology), Pythium (genetics), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Acetyltransferases, Algal Proteins, Fatty Acids, Unsaturated.
- chemical , genetics : Acetyltransferases, Algal Proteins.
- chemical , isolation & purification : Acetyltransferases, Algal Proteins.
- chemical , metabolism : Acetyltransferases, Algal Proteins, Fatty Acids, Unsaturated.
- chemistry : Pythium.
- enzymology : Pythium.
- genetics : Pythium.
- Amino Acid Motifs, Fatty Acid Elongases, Substrate Specificity.
Abstract
We describe a condensing enzyme from Pythium irregulare (PirELO) that shows highest activity on the 18-carbon, Delta-6 desaturated fatty acids, stearidonic acid and gamma-linolenic acid. However, this enzyme is also capable of elongating a number of other fatty acids including the 20-carbon, Delta-5 desaturated fatty acid eicosapentaenoic acid. Surprisingly, a Phytophthora infestans condensing enzyme (PinELO) with very high homology to PirELO did not show activity with 20-carbon fatty acids. A series of chimeric proteins for these two enzymes were constructed to investigate the influence of different regions on substrate and product length. The substitution of a region from near the center of PirELO into PinELO resulted in an enzyme having EPA-elongating activity similar to that of PirELO. Only eight amino acids differed between the two proteins in this region; however, substitution of the same region from PinELO into PirELO produced a protein which was almost inactive. The addition of a small region from near the N-terminus of PinELO was sufficient to restore activity with GLA, indicating that amino acids from these two regions interact to determine protein structure or function. Predicted topology models for PirELO and PinELO placed the two regions described here near the luminal-proximal ends of the first and fourth/fifth transmembrane helixes, at the opposite end of the condensing enzyme from four conserved regions thought to form a catalytic ring. Thus, protein characteristics determined by specific luminal-proximal regions of fatty acid condensing enzymes have a major influence on substrate specificity and final product length.
DOI: 10.1021/bi902028w
PubMed: 20397628
Affiliations:
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Vrinten</name><affiliation wicri:level="1"><nlm:affiliation>Bioriginal Food and Science Corporation, 110 Gymnasium Place, Saskatoon, Saskatchewan, Canada S7N0W9. pvrinten@bioriginal.ca</nlm:affiliation><country>Canada</country><wicri:regionArea>Bioriginal Food and Science Corporation, 110 Gymnasium Place, Saskatoon, Saskatchewan</wicri:regionArea><wicri:noRegion>Saskatchewan</wicri:noRegion></affiliation></author><author><name sortKey="Hoffman, Travis" sort="Hoffman, Travis" uniqKey="Hoffman T" first="Travis" last="Hoffman">Travis Hoffman</name></author><author><name sortKey="Bauer, Jorg" sort="Bauer, Jorg" uniqKey="Bauer J" first="Jörg" last="Bauer">Jörg Bauer</name></author><author><name sortKey="Qiu, Xiao" sort="Qiu, Xiao" uniqKey="Qiu X" first="Xiao" last="Qiu">Xiao Qiu</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20397628</idno><idno type="pmid">20397628</idno><idno type="doi">10.1021/bi902028w</idno><idno type="wicri:Area/Main/Corpus">001917</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001917</idno><idno type="wicri:Area/Main/Curation">001917</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001917</idno><idno type="wicri:Area/Main/Exploration">001917</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Specific protein regions influence substrate specificity and product length in polyunsaturated fatty acid condensing enzymes.</title><author><name sortKey="Vrinten, Patricia L" sort="Vrinten, Patricia L" uniqKey="Vrinten P" first="Patricia L" last="Vrinten">Patricia L. Vrinten</name><affiliation wicri:level="1"><nlm:affiliation>Bioriginal Food and Science Corporation, 110 Gymnasium Place, Saskatoon, Saskatchewan, Canada S7N0W9. pvrinten@bioriginal.ca</nlm:affiliation><country>Canada</country><wicri:regionArea>Bioriginal Food and Science Corporation, 110 Gymnasium Place, Saskatoon, Saskatchewan</wicri:regionArea><wicri:noRegion>Saskatchewan</wicri:noRegion></affiliation></author><author><name sortKey="Hoffman, Travis" sort="Hoffman, Travis" uniqKey="Hoffman T" first="Travis" last="Hoffman">Travis Hoffman</name></author><author><name sortKey="Bauer, Jorg" sort="Bauer, Jorg" uniqKey="Bauer J" first="Jörg" last="Bauer">Jörg Bauer</name></author><author><name sortKey="Qiu, Xiao" sort="Qiu, Xiao" uniqKey="Qiu X" first="Xiao" last="Qiu">Xiao Qiu</name></author></analytic><series><title level="j">Biochemistry</title><idno type="eISSN">1520-4995</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetyltransferases (chemistry)</term><term>Acetyltransferases (genetics)</term><term>Acetyltransferases (isolation & purification)</term><term>Acetyltransferases (metabolism)</term><term>Algal Proteins (chemistry)</term><term>Algal Proteins (genetics)</term><term>Algal Proteins (isolation & purification)</term><term>Algal Proteins (metabolism)</term><term>Amino Acid Motifs (MeSH)</term><term>Fatty Acid Elongases (MeSH)</term><term>Fatty Acids, Unsaturated (chemistry)</term><term>Fatty Acids, Unsaturated (metabolism)</term><term>Pythium (chemistry)</term><term>Pythium (enzymology)</term><term>Pythium (genetics)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acetyltransferases (composition chimique)</term><term>Acetyltransferases (génétique)</term><term>Acetyltransferases (isolement et purification)</term><term>Acetyltransferases (métabolisme)</term><term>Acides gras insaturés (composition chimique)</term><term>Acides gras insaturés (métabolisme)</term><term>Motifs d'acides aminés (MeSH)</term><term>Protéines d'algue (composition chimique)</term><term>Protéines d'algue (génétique)</term><term>Protéines d'algue (isolement et purification)</term><term>Protéines d'algue (métabolisme)</term><term>Pythium (composition chimique)</term><term>Pythium (enzymologie)</term><term>Pythium (génétique)</term><term>Spécificité du substrat (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Acetyltransferases</term><term>Algal Proteins</term><term>Fatty Acids, Unsaturated</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Acetyltransferases</term><term>Algal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Acetyltransferases</term><term>Algal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acetyltransferases</term><term>Algal Proteins</term><term>Fatty Acids, Unsaturated</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Pythium</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acetyltransferases</term><term>Acides gras insaturés</term><term>Protéines d'algue</term><term>Pythium</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Pythium</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Pythium</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Pythium</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Acetyltransferases</term><term>Protéines d'algue</term><term>Pythium</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Acetyltransferases</term><term>Protéines d'algue</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acetyltransferases</term><term>Acides gras insaturés</term><term>Protéines d'algue</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Fatty Acid Elongases</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Motifs d'acides aminés</term><term>Spécificité du substrat</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We describe a condensing enzyme from Pythium irregulare (PirELO) that shows highest activity on the 18-carbon, Delta-6 desaturated fatty acids, stearidonic acid and gamma-linolenic acid. However, this enzyme is also capable of elongating a number of other fatty acids including the 20-carbon, Delta-5 desaturated fatty acid eicosapentaenoic acid. Surprisingly, a Phytophthora infestans condensing enzyme (PinELO) with very high homology to PirELO did not show activity with 20-carbon fatty acids. A series of chimeric proteins for these two enzymes were constructed to investigate the influence of different regions on substrate and product length. The substitution of a region from near the center of PirELO into PinELO resulted in an enzyme having EPA-elongating activity similar to that of PirELO. Only eight amino acids differed between the two proteins in this region; however, substitution of the same region from PinELO into PirELO produced a protein which was almost inactive. The addition of a small region from near the N-terminus of PinELO was sufficient to restore activity with GLA, indicating that amino acids from these two regions interact to determine protein structure or function. Predicted topology models for PirELO and PinELO placed the two regions described here near the luminal-proximal ends of the first and fourth/fifth transmembrane helixes, at the opposite end of the condensing enzyme from four conserved regions thought to form a catalytic ring. Thus, protein characteristics determined by specific luminal-proximal regions of fatty acid condensing enzymes have a major influence on substrate specificity and final product length.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20397628</PMID><DateCompleted><Year>2010</Year><Month>05</Month><Day>25</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN><JournalIssue CitedMedium="Internet"><Volume>49</Volume><Issue>18</Issue><PubDate><Year>2010</Year><Month>May</Month><Day>11</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Specific protein regions influence substrate specificity and product length in polyunsaturated fatty acid condensing enzymes.</ArticleTitle><Pagination><MedlinePgn>3879-86</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/bi902028w</ELocationID><Abstract><AbstractText>We describe a condensing enzyme from Pythium irregulare (PirELO) that shows highest activity on the 18-carbon, Delta-6 desaturated fatty acids, stearidonic acid and gamma-linolenic acid. However, this enzyme is also capable of elongating a number of other fatty acids including the 20-carbon, Delta-5 desaturated fatty acid eicosapentaenoic acid. Surprisingly, a Phytophthora infestans condensing enzyme (PinELO) with very high homology to PirELO did not show activity with 20-carbon fatty acids. A series of chimeric proteins for these two enzymes were constructed to investigate the influence of different regions on substrate and product length. The substitution of a region from near the center of PirELO into PinELO resulted in an enzyme having EPA-elongating activity similar to that of PirELO. Only eight amino acids differed between the two proteins in this region; however, substitution of the same region from PinELO into PirELO produced a protein which was almost inactive. The addition of a small region from near the N-terminus of PinELO was sufficient to restore activity with GLA, indicating that amino acids from these two regions interact to determine protein structure or function. Predicted topology models for PirELO and PinELO placed the two regions described here near the luminal-proximal ends of the first and fourth/fifth transmembrane helixes, at the opposite end of the condensing enzyme from four conserved regions thought to form a catalytic ring. Thus, protein characteristics determined by specific luminal-proximal regions of fatty acid condensing enzymes have a major influence on substrate specificity and final product length.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vrinten</LastName><ForeName>Patricia L</ForeName><Initials>PL</Initials><AffiliationInfo><Affiliation>Bioriginal Food and Science Corporation, 110 Gymnasium Place, Saskatoon, Saskatchewan, Canada S7N0W9. pvrinten@bioriginal.ca</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hoffman</LastName><ForeName>Travis</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Bauer</LastName><ForeName>Jörg</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Qiu</LastName><ForeName>Xiao</ForeName><Initials>X</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020418">Algal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005231">Fatty Acids, Unsaturated</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.1.-</RegistryNumber><NameOfSubstance UI="D000123">Acetyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.1.-</RegistryNumber><NameOfSubstance UI="D000081031">Fatty Acid Elongases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000123" MajorTopicYN="N">Acetyltransferases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020418" MajorTopicYN="N">Algal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000081031" MajorTopicYN="N">Fatty Acid Elongases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005231" MajorTopicYN="N">Fatty Acids, Unsaturated</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011775" MajorTopicYN="N">Pythium</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>4</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>4</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>5</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20397628</ArticleId><ArticleId IdType="doi">10.1021/bi902028w</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country></list><tree><noCountry><name sortKey="Bauer, Jorg" sort="Bauer, Jorg" uniqKey="Bauer J" first="Jörg" last="Bauer">Jörg Bauer</name><name sortKey="Hoffman, Travis" sort="Hoffman, Travis" uniqKey="Hoffman T" first="Travis" last="Hoffman">Travis Hoffman</name><name sortKey="Qiu, Xiao" sort="Qiu, Xiao" uniqKey="Qiu X" first="Xiao" last="Qiu">Xiao Qiu</name></noCountry><country name="Canada"><noRegion><name sortKey="Vrinten, Patricia L" sort="Vrinten, Patricia L" uniqKey="Vrinten P" first="Patricia L" last="Vrinten">Patricia L. 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