Enzymatic hydrolysis of alpha- and beta-oligo(L-aspartic acid)s by poly(aspartic acid) hydrolases-1 and 2 from Sphingomonas sp. KT-1.
Identifieur interne : 000308 ( Ncbi/Merge ); précédent : 000307; suivant : 000309Enzymatic hydrolysis of alpha- and beta-oligo(L-aspartic acid)s by poly(aspartic acid) hydrolases-1 and 2 from Sphingomonas sp. KT-1.
Auteurs : Tomohiro Hiraishi [Japon] ; Mariko Kajiyama ; Ichiro Yamato ; Yoshiharu DoiSource :
- Macromolecular bioscience [ 1616-5187 ] ; 2004.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Sphingomonas.
- métabolisme : Oligopeptides, Peptides, Protéines.
- Acide aspartique, Biopolymères, Cinétique, Hydrolyse, Oligopeptides, Peptides, Protéines, Serine endopeptidases.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Oligopeptides, Peptides, Proteins, Serine Endopeptidases.
- chemical , metabolism : Oligopeptides, Peptides, Proteins.
- chemical : Aspartic Acid, Biopolymers.
- enzymology : Sphingomonas.
- Hydrolysis, Kinetics.
Abstract
The enzymatic hydrolysis of alpha- and beta-oligo(L-aspartic acid)s by PAA hydrolase-1 and PAA hydrolase-2 (purified from Sphingomonas sp. KT-1) was performed to elucidate the mechanism of the microbial degradation by Sphingomonas sp. KT-1 of the thermally synthesized alpha,beta-poly(D,L-aspartic acid) (tPAA). GPC analysis of the hydrolyzed products of alpha- and beta-tetra(L-aspartic acid)s by PAA hydrolase-1 has showed that PAA hydrolase-1 is capable of hydrolyzing only the specific amide bonds between beta-aspartic acid units. The RP-HPLC analysis of the enzymatic hydrolysis of beta-oligo(L-aspartic acid)s (4 and 5 mers) by PAA hydrolase-1 has suggested that the enzymatic hydrolysis of beta-oligo(L-aspartic acid)s occurs via an endo-mode cleavage. In contrast, PAA hydrolase-2 hydrolyzed both alpha- and beta-oligo(L-aspartic acid)s via an exo-mode cleavage to yield L-aspartic acid as a final product. A kinetic study on the enzymatic hydrolysis of alpha-oligo(L-aspartic acid)s (3 to 7 mers) by PAA hydrolase-2 has indicated that Km values are almost independent of the number of monomer units in oligomers of 4 to 7 mers, while that Vmax values are markedly dependent on the chain length and show a maximum value at 5 mer.
DOI: 10.1002/mabi.200300085
PubMed: 15468224
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KT-1.</title><author><name sortKey="Hiraishi, Tomohiro" sort="Hiraishi, Tomohiro" uniqKey="Hiraishi T" first="Tomohiro" last="Hiraishi">Tomohiro Hiraishi</name><affiliation wicri:level="1"><nlm:affiliation>Polymer Chemistry Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. thiraish@postman.riken.go.jp</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Polymer Chemistry Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198</wicri:regionArea><wicri:noRegion>Saitama 351-0198</wicri:noRegion></affiliation></author><author><name sortKey="Kajiyama, Mariko" sort="Kajiyama, Mariko" uniqKey="Kajiyama M" first="Mariko" last="Kajiyama">Mariko Kajiyama</name></author><author><name sortKey="Yamato, Ichiro" sort="Yamato, Ichiro" uniqKey="Yamato I" first="Ichiro" last="Yamato">Ichiro Yamato</name></author><author><name sortKey="Doi, Yoshiharu" sort="Doi, Yoshiharu" uniqKey="Doi Y" first="Yoshiharu" last="Doi">Yoshiharu Doi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:15468224</idno><idno type="pmid">15468224</idno><idno type="doi">10.1002/mabi.200300085</idno><idno type="wicri:Area/PubMed/Corpus">002367</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002367</idno><idno type="wicri:Area/PubMed/Curation">002367</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002367</idno><idno type="wicri:Area/PubMed/Checkpoint">002268</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002268</idno><idno type="wicri:Area/Ncbi/Merge">000308</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Enzymatic hydrolysis of alpha- and beta-oligo(L-aspartic acid)s by poly(aspartic acid) hydrolases-1 and 2 from Sphingomonas sp. KT-1.</title><author><name sortKey="Hiraishi, Tomohiro" sort="Hiraishi, Tomohiro" uniqKey="Hiraishi T" first="Tomohiro" last="Hiraishi">Tomohiro Hiraishi</name><affiliation wicri:level="1"><nlm:affiliation>Polymer Chemistry Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. thiraish@postman.riken.go.jp</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Polymer Chemistry Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198</wicri:regionArea><wicri:noRegion>Saitama 351-0198</wicri:noRegion></affiliation></author><author><name sortKey="Kajiyama, Mariko" sort="Kajiyama, Mariko" uniqKey="Kajiyama M" first="Mariko" last="Kajiyama">Mariko Kajiyama</name></author><author><name sortKey="Yamato, Ichiro" sort="Yamato, Ichiro" uniqKey="Yamato I" first="Ichiro" last="Yamato">Ichiro Yamato</name></author><author><name sortKey="Doi, Yoshiharu" sort="Doi, Yoshiharu" uniqKey="Doi Y" first="Yoshiharu" last="Doi">Yoshiharu Doi</name></author></analytic><series><title level="j">Macromolecular bioscience</title><idno type="ISSN">1616-5187</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aspartic Acid</term><term>Biopolymers</term><term>Hydrolysis</term><term>Kinetics</term><term>Oligopeptides (chemistry)</term><term>Oligopeptides (metabolism)</term><term>Peptides (chemistry)</term><term>Peptides (metabolism)</term><term>Proteins (chemistry)</term><term>Proteins (metabolism)</term><term>Serine Endopeptidases (chemistry)</term><term>Sphingomonas (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide aspartique</term><term>Biopolymères</term><term>Cinétique</term><term>Hydrolyse</term><term>Oligopeptides ()</term><term>Oligopeptides (métabolisme)</term><term>Peptides ()</term><term>Peptides (métabolisme)</term><term>Protéines ()</term><term>Protéines (métabolisme)</term><term>Serine endopeptidases ()</term><term>Sphingomonas (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oligopeptides</term><term>Peptides</term><term>Proteins</term><term>Serine Endopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oligopeptides</term><term>Peptides</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Aspartic Acid</term><term>Biopolymers</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Sphingomonas</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Sphingomonas</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oligopeptides</term><term>Peptides</term><term>Protéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrolysis</term><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acide aspartique</term><term>Biopolymères</term><term>Cinétique</term><term>Hydrolyse</term><term>Oligopeptides</term><term>Peptides</term><term>Protéines</term><term>Serine endopeptidases</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The enzymatic hydrolysis of alpha- and beta-oligo(L-aspartic acid)s by PAA hydrolase-1 and PAA hydrolase-2 (purified from Sphingomonas sp. KT-1) was performed to elucidate the mechanism of the microbial degradation by Sphingomonas sp. KT-1 of the thermally synthesized alpha,beta-poly(D,L-aspartic acid) (tPAA). GPC analysis of the hydrolyzed products of alpha- and beta-tetra(L-aspartic acid)s by PAA hydrolase-1 has showed that PAA hydrolase-1 is capable of hydrolyzing only the specific amide bonds between beta-aspartic acid units. The RP-HPLC analysis of the enzymatic hydrolysis of beta-oligo(L-aspartic acid)s (4 and 5 mers) by PAA hydrolase-1 has suggested that the enzymatic hydrolysis of beta-oligo(L-aspartic acid)s occurs via an endo-mode cleavage. In contrast, PAA hydrolase-2 hydrolyzed both alpha- and beta-oligo(L-aspartic acid)s via an exo-mode cleavage to yield L-aspartic acid as a final product. A kinetic study on the enzymatic hydrolysis of alpha-oligo(L-aspartic acid)s (3 to 7 mers) by PAA hydrolase-2 has indicated that Km values are almost independent of the number of monomer units in oligomers of 4 to 7 mers, while that Vmax values are markedly dependent on the chain length and show a maximum value at 5 mer.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15468224</PMID><DateCompleted><Year>2005</Year><Month>04</Month><Day>21</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1616-5187</ISSN><JournalIssue CitedMedium="Print"><Volume>4</Volume><Issue>3</Issue><PubDate><Year>2004</Year><Month>Mar</Month><Day>15</Day></PubDate></JournalIssue><Title>Macromolecular bioscience</Title><ISOAbbreviation>Macromol Biosci</ISOAbbreviation></Journal><ArticleTitle>Enzymatic hydrolysis of alpha- and beta-oligo(L-aspartic acid)s by poly(aspartic acid) hydrolases-1 and 2 from Sphingomonas sp. KT-1.</ArticleTitle><Pagination><MedlinePgn>330-9</MedlinePgn></Pagination><Abstract><AbstractText>The enzymatic hydrolysis of alpha- and beta-oligo(L-aspartic acid)s by PAA hydrolase-1 and PAA hydrolase-2 (purified from Sphingomonas sp. KT-1) was performed to elucidate the mechanism of the microbial degradation by Sphingomonas sp. KT-1 of the thermally synthesized alpha,beta-poly(D,L-aspartic acid) (tPAA). GPC analysis of the hydrolyzed products of alpha- and beta-tetra(L-aspartic acid)s by PAA hydrolase-1 has showed that PAA hydrolase-1 is capable of hydrolyzing only the specific amide bonds between beta-aspartic acid units. The RP-HPLC analysis of the enzymatic hydrolysis of beta-oligo(L-aspartic acid)s (4 and 5 mers) by PAA hydrolase-1 has suggested that the enzymatic hydrolysis of beta-oligo(L-aspartic acid)s occurs via an endo-mode cleavage. In contrast, PAA hydrolase-2 hydrolyzed both alpha- and beta-oligo(L-aspartic acid)s via an exo-mode cleavage to yield L-aspartic acid as a final product. A kinetic study on the enzymatic hydrolysis of alpha-oligo(L-aspartic acid)s (3 to 7 mers) by PAA hydrolase-2 has indicated that Km values are almost independent of the number of monomer units in oligomers of 4 to 7 mers, while that Vmax values are markedly dependent on the chain length and show a maximum value at 5 mer.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hiraishi</LastName><ForeName>Tomohiro</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Polymer Chemistry Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. thiraish@postman.riken.go.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kajiyama</LastName><ForeName>Mariko</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Yamato</LastName><ForeName>Ichiro</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Doi</LastName><ForeName>Yoshiharu</ForeName><Initials>Y</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>Germany</Country><MedlineTA>Macromol Biosci</MedlineTA><NlmUniqueID>101135941</NlmUniqueID><ISSNLinking>1616-5187</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001704">Biopolymers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009842">Oligopeptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C499773">alpha,beta-poly(aspartic acid)</NameOfSubstance></Chemical><Chemical><RegistryNumber>26063-13-8</RegistryNumber><NameOfSubstance UI="C017645">polyaspartate</NameOfSubstance></Chemical><Chemical><RegistryNumber>30KYC7MIAI</RegistryNumber><NameOfSubstance UI="D001224">Aspartic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="D012697">Serine Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="C473051">poly(aspartic acid) hydrolase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001224" MajorTopicYN="N">Aspartic Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001704" MajorTopicYN="N">Biopolymers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009842" MajorTopicYN="N">Oligopeptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012697" MajorTopicYN="N">Serine Endopeptidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020578" MajorTopicYN="N">Sphingomonas</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>10</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>4</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>10</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15468224</ArticleId><ArticleId IdType="doi">10.1002/mabi.200300085</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Doi, Yoshiharu" sort="Doi, Yoshiharu" uniqKey="Doi Y" first="Yoshiharu" last="Doi">Yoshiharu Doi</name><name sortKey="Kajiyama, Mariko" sort="Kajiyama, Mariko" uniqKey="Kajiyama M" first="Mariko" last="Kajiyama">Mariko Kajiyama</name><name sortKey="Yamato, Ichiro" sort="Yamato, Ichiro" uniqKey="Yamato I" first="Ichiro" last="Yamato">Ichiro Yamato</name></noCountry><country name="Japon"><noRegion><name sortKey="Hiraishi, Tomohiro" sort="Hiraishi, Tomohiro" uniqKey="Hiraishi T" first="Tomohiro" last="Hiraishi">Tomohiro Hiraishi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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