Association of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus

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dc.contributor.authorT Y Jung-
dc.contributor.authorD Li-
dc.contributor.authorJ T Park-
dc.contributor.authorS M Yoon-
dc.contributor.authorP L Tran-
dc.contributor.authorB H Oh-
dc.contributor.authorS Janecek-
dc.contributor.authorSung Goo Park-
dc.contributor.authorEui-Jeon Woo-
dc.contributor.authorK H Park-
dc.date.accessioned2017-04-19T09:29:04Z-
dc.date.available2017-04-19T09:29:04Z-
dc.date.issued2012-
dc.identifier.issn0021-9258-
dc.identifier.uri10.1074/jbc.M111.304774ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10638-
dc.description.abstractStaphylothermus marinus maltogenic amylase (SMMA) is a novel extreme thermophile maltogenic amylase with an optimal temperature of 100 °C, which hydrolyzes α-(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-loopstrand region forming a part of the substrate binding pocket with several aromatic residues, including Phe-95, Phe-96, and Tyr-99.Astructural 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 with in a monomeric subunit. The SMMA structure provides a molecular basis for the functional properties that are unique to hyperthermophile maltogenic amylases from archaea and that distinguish SMMA from moderate thermophilic or mesophilic bacterial enzymes.-
dc.publisherAmer Soc Biochemistry Molecular Biology Inc-
dc.titleAssociation of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus-
dc.title.alternativeAssociation of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus-
dc.typeArticle-
dc.citation.titleJournal of Biological Chemistry-
dc.citation.number11-
dc.citation.endPage7989-
dc.citation.startPage7979-
dc.citation.volume287-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.affiliatedAuthorEui-Jeon Woo-
dc.contributor.alternativeName정태양-
dc.contributor.alternativeName이단-
dc.contributor.alternativeName박종태-
dc.contributor.alternativeName윤세미-
dc.contributor.alternativeNameTran-
dc.contributor.alternativeName오병하-
dc.contributor.alternativeNameJanecek-
dc.contributor.alternativeName박성구-
dc.contributor.alternativeName우의전-
dc.contributor.alternativeName박관화-
dc.identifier.bibliographicCitationJournal of Biological Chemistry, vol. 287, no. 11, pp. 7979-7989-
dc.identifier.doi10.1074/jbc.M111.304774-
dc.description.journalClassY-
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Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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