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| http://purl.uniprot.org/citations/16794344 | http://www.w3.org/2000/01/rdf-schema#comment | "Di-N-acetylchitobiase is a family 18 glycoside hydrolase that splits the reducing-end GlcNAc from chitooligosaccharides. The enzyme hydrolyzed only the alpha-anomer of five tested substrates, chitin di-through hexasaccharide. In all cases the glycosyl fragment retained its beta-configuration while the split monosaccharide was alpha-D-GlcNAc. Chitobiose was hydrolyzed less than half as fast as the other larger substrates. All four of them, tri-to hexasaccharide, reacted at the same rate. The biochemical behavior of di-N-acetylchitobiase indicates it has three subsites, -2, -1, +1, in which the reducing-end trimer of any sized chitooligosaccharide is bound. The +1 site is specific for an alpha-anomer."xsd:string |
| http://purl.uniprot.org/citations/16794344 | http://purl.org/dc/terms/identifier | "doi:10.1271/bbb.60183"xsd:string |
| http://purl.uniprot.org/citations/16794344 | http://purl.uniprot.org/core/author | "Halloran B.A."xsd:string |
| http://purl.uniprot.org/citations/16794344 | http://purl.uniprot.org/core/author | "Aronson N.N."xsd:string |
| http://purl.uniprot.org/citations/16794344 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16794344 | http://purl.uniprot.org/core/name | "Biosci Biotechnol Biochem"xsd:string |
| http://purl.uniprot.org/citations/16794344 | http://purl.uniprot.org/core/pages | "1537-1541"xsd:string |
| http://purl.uniprot.org/citations/16794344 | http://purl.uniprot.org/core/title | "Optimum substrate size and specific anomer requirements for the reducing-end glycoside hydrolase di-N-acetylchitobiase."xsd:string |
| http://purl.uniprot.org/citations/16794344 | http://purl.uniprot.org/core/volume | "70"xsd:string |
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