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dc.contributor.authorEide, Kristine Bistrup
dc.contributor.authorNorberg, Anne Line
dc.contributor.authorHeggset, Ellinor Bævre
dc.contributor.authorLindbom, Anne Rita
dc.contributor.authorVårum, Kjell Morten
dc.contributor.authorEijsink, Vincent
dc.contributor.authorSørlie, Morten
dc.date.accessioned2017-10-26T07:48:01Z
dc.date.available2017-10-26T07:48:01Z
dc.date.created2012-02-23T10:37:01Z
dc.date.issued2012
dc.identifier.citationBiochemistry. 2012, 51 (1), 487-495.nb_NO
dc.identifier.issn1520-4995
dc.identifier.urihttp://hdl.handle.net/11250/2462259
dc.description.abstractChitotriosidase (HCHT) is one of two family 18 chitinases produced by humans, the other being acidic mammalian chitinase (AMCase). The enzyme is thought to be part of the human defense mechanism against fungal parasites, but its precise role and the details of its enzymatic properties have not yet been fully unraveled. We have studied the properties of HCHT by analyzing how the enzyme acts on high-molecular weight chitosans, soluble copolymers of β-1,4-linked N-acetylglucosamine (GlcNAc, A), and glucosamine (GlcN, D). Using methods for in-depth studies of the chitinolytic machinery of bacterial family 18 enzymes, we show that HCHT degrades chitosan primarily via an endoprocessive mechanism, as would be expected on the basis of the structural features of its substrate-binding cleft. The preferences of HCHT subsites for acetylated versus nonacetylated sugars were assessed by sequence analysis of obtained oligomeric products showing a very strong, absolute, and a relative weak preference for an acetylated unit in the −2, −1, and +1 subsites, respectively. The latter information is important for the design of inhibitors that are specific for the human chitinases and also provides insight into what kind of products may be formed in vivo upon administration of chitosan-containing medicines or food products.nb_NO
dc.language.isoengnb_NO
dc.publisherAmerican Chemical Societynb_NO
dc.titleHuman chitotriosidase-catalyzed hydrolysis of chitosannb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.description.versionacceptedVersionnb_NO
dc.source.pagenumber487-495nb_NO
dc.source.volume51nb_NO
dc.source.journalBiochemistrynb_NO
dc.source.issue1nb_NO
dc.identifier.doi10.1021/bi2015585
dc.identifier.cristin911335
dc.relation.projectNorges forskningsråd: 209335nb_NO
dc.description.localcodeCopyright © 2012 American Chemical Society. This is the authors’ accepted and refereed manuscript to the article.nb_NO
cristin.unitcode194,66,15,0
cristin.unitnameInstitutt for bioteknologi og matvitenskap
cristin.ispublishedtrue
cristin.fulltextpostprint
cristin.qualitycode1


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