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http://purl.uniprot.org/citations/16762038http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16762038http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16762038http://www.w3.org/2000/01/rdf-schema#comment"The gram-positive soil bacterium Cellulomonas fimi is shown to produce at least two intracellular beta-N-acetylglucosaminidases, a family 20 beta-N-acetylhexosaminidase (Hex20), and a novel family 3-beta-N-acetylglucosaminidase/beta-glucosidase (Nag3), through screening of a genomic expression library, cloning of genes and analysis of their sequences. Nag3 exhibits broad substrate specificity for substituents at the C2 position of the glycone: kcat/Km values at 25 degrees C were 0.066 s(-1) x mM(-1) and 0.076 s(-1) x mM(-1) for 4'-nitrophenyl beta-N-acetyl-D-glucosaminide and 4'-nitrophenyl beta-D-glucoside, respectively. The first glycosidase with this broad specificity to be described, Nag3, suggests an interesting evolutionary link between beta-N-acetylglucosaminidases and beta-glucosidases of family 3. Reaction by a double-displacement mechanism was confirmed for Nag3 through the identification of a glycosyl-enzyme species trapped with the slow substrate 2',4'-dinitrophenyl 2-deoxy-2-fluoro-beta-D-glucopyranoside. Hex20 requires the acetamido group at C2 of the substrate, being unable to cleave beta-glucosides, since its mechanism involves an oxazolinium ion intermediate. However, it is broad in its specificity for the D-glucosyl/D-galactosyl configuration of the glycone: Km and kcat values were 53 microM and 482.3 s(-1) for 4'-nitrophenyl beta-N-acetyl-D-glucosaminide and 66 microM and 129.1 s(-1) for 4'-nitrophenyl beta-N-acetyl-D-galactosaminide."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.org/dc/terms/identifier"doi:10.1111/j.1742-4658.2006.05308.x"xsd:string
http://purl.uniprot.org/citations/16762038http://purl.org/dc/terms/identifier"doi:10.1111/j.1742-4658.2006.05308.x"xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Mayer C."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Mayer C."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Withers S.G."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Withers S.G."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Vocadlo D.J."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Vocadlo D.J."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Rupitz K."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Rupitz K."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Warren R.A.J."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Warren R.A.J."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Stoll D."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Stoll D."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Mah M."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/author"Mah M."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/name"FEBS J."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/name"FEBS J."xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/pages"2929-2941"xsd:string
http://purl.uniprot.org/citations/16762038http://purl.uniprot.org/core/pages"2929-2941"xsd:string