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 : 003098 ( Main/Merge ); précédent : 003097; suivant : 003099Enzymatic 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><idno type="wicri:Area/Ncbi/Curation">000308</idno><idno type="wicri:Area/Ncbi/Checkpoint">000308</idno><idno type="wicri:doubleKey">1616-5187:2004:Hiraishi T:enzymatic:hydrolysis:of</idno><idno type="wicri:Area/Main/Merge">003098</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></record>Pour manipuler ce document sous Unix (Dilib)
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