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| pubmed-article:9687451 | lifeskim:mentions | umls-concept:C0598888 | lld:lifeskim |
| pubmed-article:9687451 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:9687451 | lifeskim:mentions | umls-concept:C1516050 | lld:lifeskim |
| pubmed-article:9687451 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:9687451 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:9687451 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:9687451 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:9687451 | pubmed:dateCreated | 1998-9-24 | lld:pubmed |
| pubmed-article:9687451 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9687451 | pubmed:abstractText | A beta-N-acetylglucosaminidase gene (nagA) of Streptomyces thermoviolaceus OPC-520 was cloned in Streptomyces lividans 66. The nucleotide sequence of the gene, which encodes NagA, revealed an open reading frame of 1,896 bp, encoding a protein with an Mr of 66, 329. The deduced primary structure of NagA was confirmed by comparison with the N-terminal amino acid sequence of the cloned beta-N-acetylglucosaminidase expressed by S. lividans. The enzyme shares no sequence similarity with the classical beta-N-acetylglucosaminidases belonging to family 20. However, NagA, which showed no detectable beta-glucosidase activity, revealed homology with microbial beta-glucosidases belonging to family 3; in particular, striking homology with the active-site regions of beta-glucosidases was observed. Thus, the above-mentioned results indicate that NagA from S. thermoviolaceus OPC-520 is classified as a family 3 glycosyl hydrolase. The enzyme activity was optimal at 60 degreesC and pH 5.0, and the apparent Km and Vmax values for p-nitrophenyl-beta-N-acetylglucosamine were 425.7 microM and 24.8 micromol min-1 mg of protein-1, respectively. | lld:pubmed |
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| pubmed-article:9687451 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9687451 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9687451 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9687451 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9687451 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9687451 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9687451 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9687451 | pubmed:issn | 0099-2240 | lld:pubmed |
| pubmed-article:9687451 | pubmed:author | pubmed-author:MiyamotoKK | lld:pubmed |
| pubmed-article:9687451 | pubmed:author | pubmed-author:MikamiTT | lld:pubmed |
| pubmed-article:9687451 | pubmed:author | pubmed-author:InamoriYY | lld:pubmed |
| pubmed-article:9687451 | pubmed:author | pubmed-author:TsujiboHH | lld:pubmed |
| pubmed-article:9687451 | pubmed:author | pubmed-author:HatanoNN | lld:pubmed |
| pubmed-article:9687451 | pubmed:author | pubmed-author:HirasawaAA | lld:pubmed |
| pubmed-article:9687451 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9687451 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:9687451 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9687451 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9687451 | pubmed:pagination | 2920-4 | lld:pubmed |
| pubmed-article:9687451 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9687451 | pubmed:meshHeading | pubmed-meshheading:9687451-... | lld:pubmed |
| pubmed-article:9687451 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9687451 | pubmed:articleTitle | A novel beta-N-acetylglucosaminidase from Streptomyces thermoviolaceus OPC-520: gene cloning, expression, and assignment to family 3 of the glycosyl hydrolases. | lld:pubmed |
| pubmed-article:9687451 | pubmed:affiliation | Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan. tsujibo@oysun01.oups.ac.jp | lld:pubmed |
| pubmed-article:9687451 | pubmed:publicationType | Journal Article | lld:pubmed |
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