| pubmed-article:8814220 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8814220 | lifeskim:mentions | umls-concept:C0317920 | lld:lifeskim |
| pubmed-article:8814220 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:8814220 | lifeskim:mentions | umls-concept:C2248345 | lld:lifeskim |
| pubmed-article:8814220 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8814220 | pubmed:dateCreated | 1996-10-24 | lld:pubmed |
| pubmed-article:8814220 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8814220 | pubmed:abstractText | Molecular characterisation of a lytic thermoactive beta-1,3-glucanase from Oerskovia xanthineolytica LL-G109 has been performed. A molecular mass of 27 195.6 +/- 1.3 Da and an isoelectric point of 4.85 were determined by electrospray mass spectrometry and from its titration curve, respectively. Its thermoactivity profile shows it to be a heat-stable enzyme with a temperature optimum of 65 degrees C. The secondary structure content of the protein was estimated by circular dichroism to be approx. 25% alpha-helix, 7% random coil, and 68% beta-sheet and beta-turn structure. Nuclear magnetic resonance spectra confirm the high content of beta-structure. Furthermore, the presence of a compact hydrophobic core is indicated by the presence of slowly exchanging amide hydrogens and the enzyme's relatively high resistance to proteolysis. The N-terminal sequences of the intact protein and of a tryptic peptide each exhibit significant similarity to family 16 of glycosyl hydrolases whose overall fold is known to contain almost exclusively beta-sheets and surface loops. Moreover, the sequenced tryptic peptide appears to encompass residues of the Oerskovia xanthineolytica glucanase active site, since it contains a portion of the family 16 active-site motif E-[L/I/V]-D-[L/I/V]-E. | lld:pubmed |
| pubmed-article:8814220 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8814220 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8814220 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8814220 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8814220 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8814220 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8814220 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8814220 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8814220 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:8814220 | pubmed:author | pubmed-author:DobsonC MCM | lld:pubmed |
| pubmed-article:8814220 | pubmed:author | pubmed-author:AsenjoJ AJA | lld:pubmed |
| pubmed-article:8814220 | pubmed:author | pubmed-author:KotinJJ | lld:pubmed |
| pubmed-article:8814220 | pubmed:author | pubmed-author:PontingC PCP | lld:pubmed |
| pubmed-article:8814220 | pubmed:author | pubmed-author:ParradoJJ | lld:pubmed |
| pubmed-article:8814220 | pubmed:author | pubmed-author:Conejero-Lara... | lld:pubmed |
| pubmed-article:8814220 | pubmed:author | pubmed-author:EscuredoP RPR | lld:pubmed |
| pubmed-article:8814220 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8814220 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:8814220 | pubmed:volume | 1296 | lld:pubmed |
| pubmed-article:8814220 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8814220 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8814220 | pubmed:pagination | 145-51 | lld:pubmed |
| pubmed-article:8814220 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:meshHeading | pubmed-meshheading:8814220-... | lld:pubmed |
| pubmed-article:8814220 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8814220 | pubmed:articleTitle | Molecular characterisation of a thermoactive beta-1,3-glucanase from Oerskovia xanthineolytica. | lld:pubmed |
| pubmed-article:8814220 | pubmed:affiliation | New Chemistry Laboratory, University of Oxford, UK. | lld:pubmed |
| pubmed-article:8814220 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8814220 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8814220 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8814220 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8814220 | lld:pubmed |
