Association of Novel Domain in Active Site of Archaic Hyperthermophilic Maltogenic Amylase from Staphylothermus marinus

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dc.contributor.authorJung, Tae-Yangko
dc.contributor.authorLi, Danko
dc.contributor.authorPark, Jong-Taeko
dc.contributor.authorYoon, Se-Miko
dc.contributor.authorTran, PLko
dc.contributor.authorOh, Byung-Hako
dc.contributor.authorJanecek, Stefanko
dc.contributor.authorPark, Sung Gooko
dc.contributor.authorWoo, Eui-Jeonko
dc.contributor.authorPark, Kwan-Hwako
dc.date.accessioned2013-03-13T01:52:15Z-
dc.date.available2013-03-13T01:52:15Z-
dc.date.created2012-10-25-
dc.date.created2012-10-25-
dc.date.issued2012-03-
dc.identifier.citationJOURNAL OF BIOLOGICAL CHEMISTRY, v.287, no.11, pp.7979 - 7989-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10203/104165-
dc.description.abstractStaphylothermus marinus maltogenic amylase (SMMA) is a novel extreme thermophile maltogenic amylase with an optimal temperature of 100 degrees C, which hydrolyzes alpha-(1-4)-glycosyl linkages in cyclodextrins and in linear malto-oligosaccharides. This enzyme has along N-terminal extension that is conserved among archaic hyperthermophilic amylases but is not found in other hydrolyzing enzymes from the glycoside hydrolase 13 family. The SMMA crystal structure revealed that the N-terminal extension forms an N' domain that is similar to carbohydrate-binding module 48, with the strand-loop-strand region forming a part of the substrate binding pocket with several aromatic residues, including Phe-95, Phe-96, andTyr-99. A structural comparison with conventional cyclodextrin-hydrolyzing enzymes revealed a striking resemblance between the SMMA N' domain position and the dimeric N domain position in bacterial enzymes. This result suggests that extremophilic archaea that live at high temperatures may have adopted a novel domain arrangement that combines all of the substrate binding components within a monomeric subunit. The SMMA structure provides a molecular basis for the functional properties that are unique to hyperthermophile malto-genic amylases from archaea and that distinguish SMMA from moderate thermophilic or mesophilic bacterial enzymes.-
dc.languageEnglish-
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC-
dc.subjectSTARCH-BINDING DOMAIN-
dc.subjectBACILLUS-STEAROTHERMOPHILUS NEOPULLULANASE-
dc.subjectVULGARIS R-47 ALPHA-AMYLASE-1-
dc.subjectCOMPLETE GENOME SEQUENCE-
dc.subjectFAMILY 11 XYLANASE-
dc.subjectALPHA-AMYLASE-
dc.subjectCRYSTAL-STRUCTURE-
dc.subjectSULFOLOBUS-SOLFATARICUS-
dc.subject3-DIMENSIONAL STRUCTURE-
dc.subjectPYROCOCCUS-FURIOSUS-
dc.titleAssociation of Novel Domain in Active Site of Archaic Hyperthermophilic Maltogenic Amylase from Staphylothermus marinus-
dc.typeArticle-
dc.identifier.wosid000301349400014-
dc.identifier.scopusid2-s2.0-84863239712-
dc.type.rimsART-
dc.citation.volume287-
dc.citation.issue11-
dc.citation.beginningpage7979-
dc.citation.endingpage7989-
dc.citation.publicationnameJOURNAL OF BIOLOGICAL CHEMISTRY-
dc.identifier.doi10.1074/jbc.M111.304774-
dc.contributor.localauthorOh, Byung-Ha-
dc.contributor.nonIdAuthorJung, Tae-Yang-
dc.contributor.nonIdAuthorLi, Dan-
dc.contributor.nonIdAuthorPark, Jong-Tae-
dc.contributor.nonIdAuthorYoon, Se-Mi-
dc.contributor.nonIdAuthorTran, PL-
dc.contributor.nonIdAuthorJanecek, Stefan-
dc.contributor.nonIdAuthorPark, Sung Goo-
dc.contributor.nonIdAuthorWoo, Eui-Jeon-
dc.contributor.nonIdAuthorPark, Kwan-Hwa-
dc.type.journalArticleArticle-
dc.subject.keywordPlusSTARCH-BINDING DOMAIN-
dc.subject.keywordPlusBACILLUS-STEAROTHERMOPHILUS NEOPULLULANASE-
dc.subject.keywordPlusVULGARIS R-47 ALPHA-AMYLASE-1-
dc.subject.keywordPlusCOMPLETE GENOME SEQUENCE-
dc.subject.keywordPlusFAMILY 11 XYLANASE-
dc.subject.keywordPlusALPHA-AMYLASE-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusSULFOLOBUS-SOLFATARICUS-
dc.subject.keywordPlus3-DIMENSIONAL STRUCTURE-
dc.subject.keywordPlusPYROCOCCUS-FURIOSUS-
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