Enzymatic description of the anhydrofructose pathway of glycogen degradation II. Gene identification and characterization of the reactions catalyzed by aldos-2-ulose dehydratase that converts 1,5-anhydro-D-fructose to microthecin with ascopyrone M as the intermediate.
Identifieur interne : 000860 ( Main/Curation ); précédent : 000859; suivant : 000861Enzymatic description of the anhydrofructose pathway of glycogen degradation II. Gene identification and characterization of the reactions catalyzed by aldos-2-ulose dehydratase that converts 1,5-anhydro-D-fructose to microthecin with ascopyrone M as the intermediate.
Auteurs : Shukun Yu [Danemark]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2005.
Descripteurs français
- KwdFr :
- Catalyse (MeSH), Cétoses (sucres) (biosynthèse), Données de séquences moléculaires (MeSH), Fructose (analogues et dérivés), Fructose (métabolisme), Glycogène (métabolisme), Hydro-lyases (composition chimique), Hydro-lyases (génétique), Hydro-lyases (isolement et purification), Hydro-lyases (physiologie), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH), Terminologie comme sujet (MeSH).
- MESH :
- analogues et dérivés : Fructose.
- biosynthèse : Cétoses (sucres).
- composition chimique : Hydro-lyases.
- génétique : Hydro-lyases.
- isolement et purification : Hydro-lyases.
- métabolisme : Fructose, Glycogène.
- physiologie : Hydro-lyases.
- Catalyse, Données de séquences moléculaires, Spécificité du substrat, Séquence d'acides aminés, Terminologie comme sujet.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Catalysis (MeSH), Fructose (analogs & derivatives), Fructose (metabolism), Glycogen (metabolism), Hydro-Lyases (chemistry), Hydro-Lyases (genetics), Hydro-Lyases (isolation & purification), Hydro-Lyases (physiology), Ketoses (biosynthesis), Molecular Sequence Data (MeSH), Substrate Specificity (MeSH), Terminology as Topic (MeSH).
- MESH :
- chemical , analogs & derivatives : Fructose.
- chemical , biosynthesis : Ketoses.
- chemical , chemistry : Hydro-Lyases.
- chemical , genetics : Hydro-Lyases.
- chemical , isolation & purification : Hydro-Lyases.
- chemical , metabolism : Fructose, Glycogen.
- chemical , physiology : Hydro-Lyases.
- Amino Acid Sequence, Catalysis, Molecular Sequence Data, Substrate Specificity, Terminology as Topic.
Abstract
The anhydrofructose pathway describes the degradation of glycogen and starch to metabolites via 1,5-anhydro-D-fructose (1,5AnFru). Enzymes that form 1,5AnFru, ascopyrone P (APP), and ascopyrone M (APM) have been reported from our laboratory earlier. In the present study, APM formed from 1,5AnFru was found to be the intermediate to the antimicrobial microthecin. The microthecin forming enzyme from the fungus Phanerochaete chrysosporium proved to be aldos-2-ulose dehydratase (AUDH, EC 4.2.1.-), which was purified and characterized for its enzymatic and catalytic properties. The purified AUDH showing a molecular mass of 97.4 kDa on SDS-PAGE was partially sequenced. Total 332 amino acid residues in length were obtained, representing some 37% of the AUDH protein. The obtained amino acid sequences showed no homology to known proteins but to an unannotated DNA sequence in Scaffold 62 of the published genome of the fungus. The alignment revealed three introns of the identified AUDH gene (Audh; ph.chr), thus the first gene coding for a neutral sugar dehydratase is identified. AUDH was found to be a bi-functional enzyme, being able to dehydrate 1,5AnFru to APM and further isomerizing the APM formed to microthecin. The optimal pH for the formation of APM and microthecin was pH 5.8 and 6.8, respectively. AUDH showed 5 fold higher activity toward 1,5AnFru than toward its analogue glucosone, when tested at concentrations from 0.6 mM to 0.2 M. Based on the characteristic UV absorbance of microthecin (230 nm) and APM (262 nm) assay methods were developed for the microthecin forming enzymes.
DOI: 10.1016/j.bbagen.2005.01.004
PubMed: 15716041
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Gene identification and characterization of the reactions catalyzed by aldos-2-ulose dehydratase that converts 1,5-anhydro-D-fructose to microthecin with ascopyrone M as the intermediate.</title><author><name sortKey="Yu, Shukun" sort="Yu, Shukun" uniqKey="Yu S" first="Shukun" last="Yu">Shukun Yu</name><affiliation wicri:level="1"><nlm:affiliation>Danisco Innovation, Danisco A/S, Langebrogade 1, PO box 17, DK 1001, Copenhagen K, Denmark. g7SY@Danisco.com</nlm:affiliation><country xml:lang="fr">Danemark</country><wicri:regionArea>Danisco Innovation, Danisco A/S, Langebrogade 1, PO box 17, DK 1001, Copenhagen K</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15716041</idno><idno type="pmid">15716041</idno><idno type="doi">10.1016/j.bbagen.2005.01.004</idno><idno type="wicri:Area/Main/Corpus">000860</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000860</idno><idno type="wicri:Area/Main/Curation">000860</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000860</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Enzymatic description of the anhydrofructose pathway of glycogen degradation II. Gene identification and characterization of the reactions catalyzed by aldos-2-ulose dehydratase that converts 1,5-anhydro-D-fructose to microthecin with ascopyrone M as the intermediate.</title><author><name sortKey="Yu, Shukun" sort="Yu, Shukun" uniqKey="Yu S" first="Shukun" last="Yu">Shukun Yu</name><affiliation wicri:level="1"><nlm:affiliation>Danisco Innovation, Danisco A/S, Langebrogade 1, PO box 17, DK 1001, Copenhagen K, Denmark. g7SY@Danisco.com</nlm:affiliation><country xml:lang="fr">Danemark</country><wicri:regionArea>Danisco Innovation, Danisco A/S, Langebrogade 1, PO box 17, DK 1001, Copenhagen K</wicri:regionArea></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Catalysis (MeSH)</term><term>Fructose (analogs & derivatives)</term><term>Fructose (metabolism)</term><term>Glycogen (metabolism)</term><term>Hydro-Lyases (chemistry)</term><term>Hydro-Lyases (genetics)</term><term>Hydro-Lyases (isolation & purification)</term><term>Hydro-Lyases (physiology)</term><term>Ketoses (biosynthesis)</term><term>Molecular Sequence Data (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Terminology as Topic (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse (MeSH)</term><term>Cétoses (sucres) (biosynthèse)</term><term>Données de séquences moléculaires (MeSH)</term><term>Fructose (analogues et dérivés)</term><term>Fructose (métabolisme)</term><term>Glycogène (métabolisme)</term><term>Hydro-lyases (composition chimique)</term><term>Hydro-lyases (génétique)</term><term>Hydro-lyases (isolement et purification)</term><term>Hydro-lyases (physiologie)</term><term>Spécificité du substrat (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Terminologie comme sujet (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Fructose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Ketoses</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hydro-Lyases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Hydro-Lyases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Hydro-Lyases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fructose</term><term>Glycogen</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Hydro-Lyases</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Fructose</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Cétoses (sucres)</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Hydro-lyases</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Hydro-lyases</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Hydro-lyases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fructose</term><term>Glycogène</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Hydro-lyases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Catalysis</term><term>Molecular Sequence Data</term><term>Substrate Specificity</term><term>Terminology as Topic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Données de séquences moléculaires</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term><term>Terminologie comme sujet</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The anhydrofructose pathway describes the degradation of glycogen and starch to metabolites via 1,5-anhydro-D-fructose (1,5AnFru). Enzymes that form 1,5AnFru, ascopyrone P (APP), and ascopyrone M (APM) have been reported from our laboratory earlier. In the present study, APM formed from 1,5AnFru was found to be the intermediate to the antimicrobial microthecin. The microthecin forming enzyme from the fungus Phanerochaete chrysosporium proved to be aldos-2-ulose dehydratase (AUDH, EC 4.2.1.-), which was purified and characterized for its enzymatic and catalytic properties. The purified AUDH showing a molecular mass of 97.4 kDa on SDS-PAGE was partially sequenced. Total 332 amino acid residues in length were obtained, representing some 37% of the AUDH protein. The obtained amino acid sequences showed no homology to known proteins but to an unannotated DNA sequence in Scaffold 62 of the published genome of the fungus. The alignment revealed three introns of the identified AUDH gene (Audh; ph.chr), thus the first gene coding for a neutral sugar dehydratase is identified. AUDH was found to be a bi-functional enzyme, being able to dehydrate 1,5AnFru to APM and further isomerizing the APM formed to microthecin. The optimal pH for the formation of APM and microthecin was pH 5.8 and 6.8, respectively. AUDH showed 5 fold higher activity toward 1,5AnFru than toward its analogue glucosone, when tested at concentrations from 0.6 mM to 0.2 M. Based on the characteristic UV absorbance of microthecin (230 nm) and APM (262 nm) assay methods were developed for the microthecin forming enzymes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15716041</PMID><DateCompleted><Year>2005</Year><Month>07</Month><Day>12</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1723</Volume><Issue>1-3</Issue><PubDate><Year>2005</Year><Month>May</Month><Day>25</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Enzymatic description of the anhydrofructose pathway of glycogen degradation II. Gene identification and characterization of the reactions catalyzed by aldos-2-ulose dehydratase that converts 1,5-anhydro-D-fructose to microthecin with ascopyrone M as the intermediate.</ArticleTitle><Pagination><MedlinePgn>63-73</MedlinePgn></Pagination><Abstract><AbstractText>The anhydrofructose pathway describes the degradation of glycogen and starch to metabolites via 1,5-anhydro-D-fructose (1,5AnFru). Enzymes that form 1,5AnFru, ascopyrone P (APP), and ascopyrone M (APM) have been reported from our laboratory earlier. In the present study, APM formed from 1,5AnFru was found to be the intermediate to the antimicrobial microthecin. The microthecin forming enzyme from the fungus Phanerochaete chrysosporium proved to be aldos-2-ulose dehydratase (AUDH, EC 4.2.1.-), which was purified and characterized for its enzymatic and catalytic properties. The purified AUDH showing a molecular mass of 97.4 kDa on SDS-PAGE was partially sequenced. Total 332 amino acid residues in length were obtained, representing some 37% of the AUDH protein. The obtained amino acid sequences showed no homology to known proteins but to an unannotated DNA sequence in Scaffold 62 of the published genome of the fungus. The alignment revealed three introns of the identified AUDH gene (Audh; ph.chr), thus the first gene coding for a neutral sugar dehydratase is identified. AUDH was found to be a bi-functional enzyme, being able to dehydrate 1,5AnFru to APM and further isomerizing the APM formed to microthecin. The optimal pH for the formation of APM and microthecin was pH 5.8 and 6.8, respectively. AUDH showed 5 fold higher activity toward 1,5AnFru than toward its analogue glucosone, when tested at concentrations from 0.6 mM to 0.2 M. Based on the characteristic UV absorbance of microthecin (230 nm) and APM (262 nm) assay methods were developed for the microthecin forming enzymes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Shukun</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Danisco Innovation, Danisco A/S, Langebrogade 1, PO box 17, DK 1001, Copenhagen K, Denmark. g7SY@Danisco.com</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>01</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007661">Ketoses</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C118494">microthecin</NameOfSubstance></Chemical><Chemical><RegistryNumber>30237-26-4</RegistryNumber><NameOfSubstance UI="D005632">Fructose</NameOfSubstance></Chemical><Chemical><RegistryNumber>75414-43-6</RegistryNumber><NameOfSubstance UI="C048927">1,5-anhydrofructose</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-79-2</RegistryNumber><NameOfSubstance UI="D006003">Glycogen</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.-</RegistryNumber><NameOfSubstance UI="D006836">Hydro-Lyases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.-</RegistryNumber><NameOfSubstance UI="C082557">pyranosone dehydratase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005632" MajorTopicYN="N">Fructose</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006003" MajorTopicYN="N">Glycogen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006836" MajorTopicYN="N">Hydro-Lyases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007661" MajorTopicYN="N">Ketoses</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009626" MajorTopicYN="N">Terminology as Topic</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2004</Year><Month>06</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2005</Year><Month>01</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2005</Year><Month>01</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>2</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>7</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>2</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15716041</ArticleId><ArticleId IdType="pii">S0304-4165(05)00008-5</ArticleId><ArticleId IdType="doi">10.1016/j.bbagen.2005.01.004</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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