Critical molecular regions for elicitation of the sweetness of the sweet-tasting protein, thaumatin I.
Identifieur interne : 000349 ( Main/Exploration ); précédent : 000348; suivant : 000350Critical molecular regions for elicitation of the sweetness of the sweet-tasting protein, thaumatin I.
Auteurs : Keisuke Ohta [Japon] ; Tetsuya Masuda ; Nobuyuki Ide ; Naofumi KitabatakeSource :
- The FEBS journal [ 1742-464X ] ; 2008.
Descripteurs français
- KwdFr :
- Acides aminés basiques (génétique), Alanine (composition chimique), Alanine (génétique), Arginine (composition chimique), Arginine (génétique), Conformation des protéines (MeSH), Goût (MeSH), Lysine (composition chimique), Lysine (génétique), Modèles moléculaires (MeSH), Mutation (MeSH), Pichia (génétique), Protéines végétales (composition chimique), Protéines végétales (génétique), Protéines végétales (isolement et purification), Substitution d'acide aminé (MeSH), Édulcorants (composition chimique), Édulcorants (isolement et purification).
- MESH :
- composition chimique : Alanine, Arginine, Lysine, Protéines végétales, Édulcorants.
- génétique : Acides aminés basiques, Alanine, Arginine, Lysine, Pichia, Protéines végétales.
- isolement et purification : Protéines végétales, Édulcorants.
- Conformation des protéines, Goût, Modèles moléculaires, Mutation, Substitution d'acide aminé.
English descriptors
- KwdEn :
- Alanine (chemistry), Alanine (genetics), Amino Acid Substitution (MeSH), Amino Acids, Basic (genetics), Arginine (chemistry), Arginine (genetics), Lysine (chemistry), Lysine (genetics), Models, Molecular (MeSH), Mutation (MeSH), Pichia (genetics), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (isolation & purification), Protein Conformation (MeSH), Sweetening Agents (chemistry), Sweetening Agents (isolation & purification), Taste (MeSH).
- MESH :
- chemical , chemistry : Alanine, Arginine, Lysine, Plant Proteins, Sweetening Agents.
- chemical , genetics : Alanine, Amino Acids, Basic, Arginine, Lysine, Plant Proteins.
- genetics : Pichia.
- chemical , isolation & purification : Plant Proteins, Sweetening Agents.
- Amino Acid Substitution, Models, Molecular, Mutation, Protein Conformation, Taste.
Abstract
Thaumatin is an intensely sweet-tasting protein. To identify the critical amino acid residue(s) responsible for elicitation of the sweetness of thaumatin, we prepared mutant thaumatin proteins, using Pichia pastoris, in which alanine residues were substituted for lysine or arginine residues, and the sweetness of each mutant protein was evaluated by sensory analysis in humans. Four lysine residues (K49, K67, K106 and K163) and three arginine residues (R76, R79 and R82) played significant roles in thaumatin sweetness. Of these residues, K67 and R82 were particularly important for eliciting the sweetness. We also prepared two further mutant thaumatin I proteins: one in which an arginine residue was substituted for a lysine residue, R82K, and one in which a lysine residue was substituted for an arginine residue, K67R. The threshold value for sweetness was higher for R82K than for thaumatin I, indicating that not only the positive charge but also the structure of the side chain of the arginine residue at position 82 influences the sweetness of thaumatin, whereas only the positive charge of the K67 side chain affects sweetness.
DOI: 10.1111/j.1742-4658.2008.06509.x
PubMed: 18544096
Affiliations:
Links toward previous steps (curation, corpus...)
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thaumatin I.</title><author><name sortKey="Ohta, Keisuke" sort="Ohta, Keisuke" uniqKey="Ohta K" first="Keisuke" last="Ohta">Keisuke Ohta</name><affiliation wicri:level="4"><nlm:affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University</wicri:regionArea><placeName><settlement type="city">Kyoto</settlement><region type="prefecture">Région du Kansai</region></placeName><orgName type="university">Université de Kyoto</orgName></affiliation></author><author><name sortKey="Masuda, Tetsuya" sort="Masuda, Tetsuya" uniqKey="Masuda T" first="Tetsuya" last="Masuda">Tetsuya Masuda</name></author><author><name sortKey="Ide, Nobuyuki" sort="Ide, Nobuyuki" uniqKey="Ide N" first="Nobuyuki" last="Ide">Nobuyuki Ide</name></author><author><name sortKey="Kitabatake, Naofumi" sort="Kitabatake, Naofumi" uniqKey="Kitabatake N" first="Naofumi" last="Kitabatake">Naofumi Kitabatake</name></author></analytic><series><title level="j">The FEBS journal</title><idno type="ISSN">1742-464X</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alanine (chemistry)</term><term>Alanine (genetics)</term><term>Amino Acid Substitution (MeSH)</term><term>Amino Acids, Basic (genetics)</term><term>Arginine (chemistry)</term><term>Arginine (genetics)</term><term>Lysine (chemistry)</term><term>Lysine (genetics)</term><term>Models, Molecular (MeSH)</term><term>Mutation (MeSH)</term><term>Pichia (genetics)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (isolation & purification)</term><term>Protein Conformation (MeSH)</term><term>Sweetening Agents (chemistry)</term><term>Sweetening Agents (isolation & purification)</term><term>Taste (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés basiques (génétique)</term><term>Alanine (composition chimique)</term><term>Alanine (génétique)</term><term>Arginine (composition chimique)</term><term>Arginine (génétique)</term><term>Conformation des protéines (MeSH)</term><term>Goût (MeSH)</term><term>Lysine (composition chimique)</term><term>Lysine (génétique)</term><term>Modèles moléculaires (MeSH)</term><term>Mutation (MeSH)</term><term>Pichia (génétique)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (génétique)</term><term>Protéines végétales (isolement et purification)</term><term>Substitution d'acide aminé (MeSH)</term><term>Édulcorants (composition chimique)</term><term>Édulcorants (isolement et purification)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" 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Agents</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines végétales</term><term>Édulcorants</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Models, Molecular</term><term>Mutation</term><term>Protein Conformation</term><term>Taste</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Goût</term><term>Modèles moléculaires</term><term>Mutation</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thaumatin is an intensely sweet-tasting protein. To identify the critical amino acid residue(s) responsible for elicitation of the sweetness of thaumatin, we prepared mutant thaumatin proteins, using Pichia pastoris, in which alanine residues were substituted for lysine or arginine residues, and the sweetness of each mutant protein was evaluated by sensory analysis in humans. Four lysine residues (K49, K67, K106 and K163) and three arginine residues (R76, R79 and R82) played significant roles in thaumatin sweetness. Of these residues, K67 and R82 were particularly important for eliciting the sweetness. We also prepared two further mutant thaumatin I proteins: one in which an arginine residue was substituted for a lysine residue, R82K, and one in which a lysine residue was substituted for an arginine residue, K67R. The threshold value for sweetness was higher for R82K than for thaumatin I, indicating that not only the positive charge but also the structure of the side chain of the arginine residue at position 82 influences the sweetness of thaumatin, whereas only the positive charge of the K67 side chain affects sweetness.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18544096</PMID><DateCompleted><Year>2008</Year><Month>09</Month><Day>02</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1742-464X</ISSN><JournalIssue CitedMedium="Print"><Volume>275</Volume><Issue>14</Issue><PubDate><Year>2008</Year><Month>Jul</Month></PubDate></JournalIssue><Title>The FEBS journal</Title><ISOAbbreviation>FEBS J</ISOAbbreviation></Journal><ArticleTitle>Critical molecular regions for elicitation of the sweetness of the sweet-tasting protein, thaumatin I.</ArticleTitle><Pagination><MedlinePgn>3644-52</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1742-4658.2008.06509.x</ELocationID><Abstract><AbstractText>Thaumatin is an intensely sweet-tasting protein. To identify the critical amino acid residue(s) responsible for elicitation of the sweetness of thaumatin, we prepared mutant thaumatin proteins, using Pichia pastoris, in which alanine residues were substituted for lysine or arginine residues, and the sweetness of each mutant protein was evaluated by sensory analysis in humans. Four lysine residues (K49, K67, K106 and K163) and three arginine residues (R76, R79 and R82) played significant roles in thaumatin sweetness. Of these residues, K67 and R82 were particularly important for eliciting the sweetness. We also prepared two further mutant thaumatin I proteins: one in which an arginine residue was substituted for a lysine residue, R82K, and one in which a lysine residue was substituted for an arginine residue, K67R. The threshold value for sweetness was higher for R82K than for thaumatin I, indicating that not only the positive charge but also the structure of the side chain of the arginine residue at position 82 influences the sweetness of thaumatin, whereas only the positive charge of the K67 side chain affects sweetness.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ohta</LastName><ForeName>Keisuke</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Masuda</LastName><ForeName>Tetsuya</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Ide</LastName><ForeName>Nobuyuki</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Kitabatake</LastName><ForeName>Naofumi</ForeName><Initials>N</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS J</MedlineTA><NlmUniqueID>101229646</NlmUniqueID><ISSNLinking>1742-464X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024361">Amino Acids, Basic</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013549">Sweetening Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, 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Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013549" MajorTopicYN="N">Sweetening Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013649" MajorTopicYN="Y">Taste</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>6</Month><Day>12</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>9</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>6</Month><Day>12</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18544096</ArticleId><ArticleId IdType="pii">EJB6509</ArticleId><ArticleId IdType="doi">10.1111/j.1742-4658.2008.06509.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région du Kansai</li></region><settlement><li>Kyoto</li></settlement><orgName><li>Université de Kyoto</li></orgName></list><tree><noCountry><name sortKey="Ide, Nobuyuki" sort="Ide, Nobuyuki" uniqKey="Ide N" first="Nobuyuki" last="Ide">Nobuyuki Ide</name><name sortKey="Kitabatake, Naofumi" sort="Kitabatake, Naofumi" uniqKey="Kitabatake N" first="Naofumi" last="Kitabatake">Naofumi Kitabatake</name><name sortKey="Masuda, Tetsuya" sort="Masuda, Tetsuya" uniqKey="Masuda T" first="Tetsuya" last="Masuda">Tetsuya Masuda</name></noCountry><country name="Japon"><region name="Région du Kansai"><name sortKey="Ohta, Keisuke" sort="Ohta, Keisuke" uniqKey="Ohta K" first="Keisuke" last="Ohta">Keisuke Ohta</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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