Enzymatic properties of the sweet-tasting proteins thaumatin and monellin after partial reduction.
Identifieur interne : 000574 ( Main/Exploration ); précédent : 000573; suivant : 000575Enzymatic properties of the sweet-tasting proteins thaumatin and monellin after partial reduction.
Auteurs : H. Van Der Wel ; W J BelSource :
- European journal of biochemistry [ 0014-2956 ] ; 1980.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Plantes.
- métabolisme : Amidohydrolases, Esterases, Peptide hydrolases, Protéines végétales, Édulcorants.
- Cinétique, Disulfures, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Amidohydrolases, Esterases, Peptide Hydrolases, Plant Proteins, Sweetening Agents.
- chemical : Disulfides.
- enzymology : Plants.
- Kinetics, Oxidation-Reduction.
Abstract
After partial reduction of disulfide bonds in the thaumatins, the sweet-tasting proteins from the fruits of Thaumatococcus danielii Benth, a rapid autodigestion was demonstrated. In the presence of suitable substrates, the reduced thaumatins showed protease, amidase and esterase activity. Thiol-blocking reagents like mercury(II) chloride inhibited the enzymatic activity. Of the thaumatins b, c, I, II and III (with increasing isoelectric points), thaumatin I showed the lowest enzymatic activity. In this series, the enzymatic activity increased from thaumatin I to thaumatin III as well as from thaumatin I to thaumatin b. Acetylation of the epsilon-amino group of lysine residues in the thaumatins by acetic anhydride, causing a decrease in basicity, led to an increase in enzymatic activity, which is correlated with the number of acetyl groups introduced. Comparison of the amino acid sequence of thaumatin I with that of cysteine proteases of plant origin showed no similarities. Moreover, the thaumatins lack histidine, one of the amino acids in the active site of the cysteine proteases. Monellin, the sweet-tasting protein from the fruits of Dioscoreophyllum cumminsii Diels, is not enzymatically active. However, when monellin with acetylated epsilon-amino groups of lysine residues was brought into a reducing environment it appeared to be enzymatically active. The similarities in properties of the thaumatins and monellin suggest a structural relationship between these proteins.
DOI: 10.1111/j.1432-1033.1980.tb04442.x
PubMed: 6988215
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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In the presence of suitable substrates, the reduced thaumatins showed protease, amidase and esterase activity. Thiol-blocking reagents like mercury(II) chloride inhibited the enzymatic activity. Of the thaumatins b, c, I, II and III (with increasing isoelectric points), thaumatin I showed the lowest enzymatic activity. In this series, the enzymatic activity increased from thaumatin I to thaumatin III as well as from thaumatin I to thaumatin b. Acetylation of the epsilon-amino group of lysine residues in the thaumatins by acetic anhydride, causing a decrease in basicity, led to an increase in enzymatic activity, which is correlated with the number of acetyl groups introduced. Comparison of the amino acid sequence of thaumatin I with that of cysteine proteases of plant origin showed no similarities. Moreover, the thaumatins lack histidine, one of the amino acids in the active site of the cysteine proteases. Monellin, the sweet-tasting protein from the fruits of Dioscoreophyllum cumminsii Diels, is not enzymatically active. However, when monellin with acetylated epsilon-amino groups of lysine residues was brought into a reducing environment it appeared to be enzymatically active. The similarities in properties of the thaumatins and monellin suggest a structural relationship between these proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">6988215</PMID><DateCompleted><Year>1980</Year><Month>06</Month><Day>27</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>104</Volume><Issue>2</Issue><PubDate><Year>1980</Year><Month>Mar</Month></PubDate></JournalIssue><Title>European journal of biochemistry</Title><ISOAbbreviation>Eur J Biochem</ISOAbbreviation></Journal><ArticleTitle>Enzymatic properties of the sweet-tasting proteins thaumatin and monellin after partial reduction.</ArticleTitle><Pagination><MedlinePgn>413-8</MedlinePgn></Pagination><Abstract><AbstractText>After partial reduction of disulfide bonds in the thaumatins, the sweet-tasting proteins from the fruits of Thaumatococcus danielii Benth, a rapid autodigestion was demonstrated. In the presence of suitable substrates, the reduced thaumatins showed protease, amidase and esterase activity. Thiol-blocking reagents like mercury(II) chloride inhibited the enzymatic activity. Of the thaumatins b, c, I, II and III (with increasing isoelectric points), thaumatin I showed the lowest enzymatic activity. In this series, the enzymatic activity increased from thaumatin I to thaumatin III as well as from thaumatin I to thaumatin b. Acetylation of the epsilon-amino group of lysine residues in the thaumatins by acetic anhydride, causing a decrease in basicity, led to an increase in enzymatic activity, which is correlated with the number of acetyl groups introduced. Comparison of the amino acid sequence of thaumatin I with that of cysteine proteases of plant origin showed no similarities. Moreover, the thaumatins lack histidine, one of the amino acids in the active site of the cysteine proteases. Monellin, the sweet-tasting protein from the fruits of Dioscoreophyllum cumminsii Diels, is not enzymatically active. However, when monellin with acetylated epsilon-amino groups of lysine residues was brought into a reducing environment it appeared to be enzymatically active. The similarities in properties of the thaumatins and monellin suggest a structural relationship between these proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Van Der Wel</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Bel</LastName><ForeName>W J</ForeName><Initials>WJ</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</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="D004220">Disulfides</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>0</RegistryNumber><NameOfSubstance UI="C002541">monellin protein, Dioscoreophyllum cumminsii</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.-</RegistryNumber><NameOfSubstance UI="D004950">Esterases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010447">Peptide Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.5.-</RegistryNumber><NameOfSubstance UI="D000581">Amidohydrolases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000581" MajorTopicYN="N">Amidohydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004950" MajorTopicYN="N">Esterases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010447" MajorTopicYN="N">Peptide Hydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013549" MajorTopicYN="N">Sweetening Agents</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1980</Year><Month>3</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1980</Year><Month>3</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1980</Year><Month>3</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">6988215</ArticleId><ArticleId IdType="doi">10.1111/j.1432-1033.1980.tb04442.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Bel, W J" sort="Bel, W J" uniqKey="Bel W" first="W J" last="Bel">W J Bel</name><name sortKey="Van Der Wel, H" sort="Van Der Wel, H" uniqKey="Van Der Wel H" first="H" last="Van Der Wel">H. 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