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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2006-9-21
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pubmed:abstractText |
Group A streptococcus (Streptococcus pyogenes) is the causative agent of severe invasive infections such as necrotizing fasciitis (the so-called 'flesh eating disease') and toxic-shock syndrome. Spy1600, a glycoside hydrolase from family 84 of the large superfamily of glycoside hydrolases, has been proposed to be a virulence factor. In the present study we show that Spy1600 has no activity toward galactosaminides or hyaluronan, but does remove beta-O-linked N-acetylglucosamine from mammalian glycoproteins--an observation consistent with the inclusion of eukaryotic O-glycoprotein 2-acetamido-2-deoxy-beta-D-glucopyranosidases within glycoside hydrolase family 84. Proton NMR studies, structure-reactivity studies for a series of fluorinated analogues and analysis of 1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-Delta2'-thiazoline as a competitive inhibitor reveals that Spy1600 uses a double-displacement mechanism involving substrate-assisted catalysis. Family 84 glycoside hydrolases are therefore comprised of both prokaryotic and eukaryotic beta-N-acetylglucosaminidases using a conserved catalytic mechanism involving substrate-assisted catalysis. Since these enzymes do not have detectable hyaluronidase activity, many family 84 glycoside hydrolases are most likely incorrectly annotated as hyaluronidases.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-10885988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-11256960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-11296296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-11341771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-11532966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-12466882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-12574517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-13786642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-14681378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-15223320,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-15795231,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-16171396,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-16253886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-16533067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-16541109,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-16565725,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-16584714,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-4859245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-6421821,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-7440573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-8034696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-8177218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-9373935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-9396742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-942051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16822234-9811929
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-methylumbelliferyl-6-sulfo-2-aceta...,
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosaminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Hyaluronoglucosaminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Hymecromone,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetylglucosamine thiazoline,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles,
http://linkedlifedata.com/resource/pubmed/chemical/beta-N-Acetylhexosaminidases,
http://linkedlifedata.com/resource/pubmed/chemical/hexosaminidase C
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1470-8728
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
399
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
241-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16822234-Acetylglucosamine,
pubmed-meshheading:16822234-Acetylglucosaminidase,
pubmed-meshheading:16822234-Amino Acid Sequence,
pubmed-meshheading:16822234-Animals,
pubmed-meshheading:16822234-COS Cells,
pubmed-meshheading:16822234-Catalysis,
pubmed-meshheading:16822234-Cercopithecus aethiops,
pubmed-meshheading:16822234-Escherichia coli,
pubmed-meshheading:16822234-Histone Acetyltransferases,
pubmed-meshheading:16822234-Humans,
pubmed-meshheading:16822234-Hyaluronoglucosaminidase,
pubmed-meshheading:16822234-Hydrolysis,
pubmed-meshheading:16822234-Hymecromone,
pubmed-meshheading:16822234-Kinetics,
pubmed-meshheading:16822234-Molecular Sequence Data,
pubmed-meshheading:16822234-Multienzyme Complexes,
pubmed-meshheading:16822234-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:16822234-Sequence Homology, Amino Acid,
pubmed-meshheading:16822234-Streptococcus pyogenes,
pubmed-meshheading:16822234-Structure-Activity Relationship,
pubmed-meshheading:16822234-Substrate Specificity,
pubmed-meshheading:16822234-Thiazoles,
pubmed-meshheading:16822234-beta-N-Acetylhexosaminidases
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pubmed:year |
2006
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pubmed:articleTitle |
Functional analysis of a group A streptococcal glycoside hydrolase Spy1600 from family 84 reveals it is a beta-N-acetylglucosaminidase and not a hyaluronidase.
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pubmed:affiliation |
Biomolecular and Biomedical Research Centre, School of Applied Sciences, Northumbria University, Newcastle upon Tyne NE1 8ST, UK.
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pubmed:publicationType |
Journal Article
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