| pubmed-article:21029756 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21029756 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:21029756 | lifeskim:mentions | umls-concept:C0017977 | lld:lifeskim |
| pubmed-article:21029756 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
| pubmed-article:21029756 | lifeskim:mentions | umls-concept:C0968184 | lld:lifeskim |
| pubmed-article:21029756 | lifeskim:mentions | umls-concept:C0048584 | lld:lifeskim |
| pubmed-article:21029756 | lifeskim:mentions | umls-concept:C0968183 | lld:lifeskim |
| pubmed-article:21029756 | lifeskim:mentions | umls-concept:C0243072 | lld:lifeskim |
| pubmed-article:21029756 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:21029756 | pubmed:dateCreated | 2011-1-3 | lld:pubmed |
| pubmed-article:21029756 | pubmed:abstractText | Measurements of esterase activity by enzyme-coupled assays on monoacetates of 4-nitrophenyl ?-D-xylopyranoside and 4-nitrophenyl ?-L-arabinofuranoside showed that acetylxylan esterases of families 1, 4 and 5 produced by Trichoderma reesei and Penicillium purpurogenum have a strong preference for deacetylation of position 2 in xylopyranosides. The acetylxylan esterases exhibit only weak activity on acetylated arabinofuranosides, with 2-acetate as the best substrate. Acetyl esterases of family 16 produced by the same two fungi deacetylate in xylopyranosides preferentially positions 3 and 4. Their specific activity on arabinofuranosides is also much lower than on xylopyranosides, however, substantially greater than that in the case of typical acetylxylan esterases. | lld:pubmed |
| pubmed-article:21029756 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21029756 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21029756 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21029756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21029756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21029756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21029756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21029756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21029756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21029756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21029756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21029756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21029756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21029756 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21029756 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:21029756 | pubmed:issn | 1873-4863 | lld:pubmed |
| pubmed-article:21029756 | pubmed:author | pubmed-author:TenkanenMaija... | lld:pubmed |
| pubmed-article:21029756 | pubmed:author | pubmed-author:EyzaguirreJai... | lld:pubmed |
| pubmed-article:21029756 | pubmed:author | pubmed-author:LiXin-LiangXL | lld:pubmed |
| pubmed-article:21029756 | pubmed:author | pubmed-author:MastihubováMá... | lld:pubmed |
| pubmed-article:21029756 | pubmed:author | pubmed-author:BielyPeterP | lld:pubmed |
| pubmed-article:21029756 | pubmed:author | pubmed-author:VršanskáMária... | lld:pubmed |
| pubmed-article:21029756 | pubmed:copyrightInfo | © 2010 Elsevier B.V. All rights reserved. | lld:pubmed |
| pubmed-article:21029756 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21029756 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:21029756 | pubmed:volume | 151 | lld:pubmed |
| pubmed-article:21029756 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21029756 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21029756 | pubmed:pagination | 137-42 | lld:pubmed |
| pubmed-article:21029756 | pubmed:meshHeading | pubmed-meshheading:21029756... | lld:pubmed |
| pubmed-article:21029756 | pubmed:meshHeading | pubmed-meshheading:21029756... | lld:pubmed |
| pubmed-article:21029756 | pubmed:meshHeading | pubmed-meshheading:21029756... | lld:pubmed |
| pubmed-article:21029756 | pubmed:meshHeading | pubmed-meshheading:21029756... | lld:pubmed |
| pubmed-article:21029756 | pubmed:meshHeading | pubmed-meshheading:21029756... | lld:pubmed |
| pubmed-article:21029756 | pubmed:meshHeading | pubmed-meshheading:21029756... | lld:pubmed |
| pubmed-article:21029756 | pubmed:meshHeading | pubmed-meshheading:21029756... | lld:pubmed |
| pubmed-article:21029756 | pubmed:meshHeading | pubmed-meshheading:21029756... | lld:pubmed |
| pubmed-article:21029756 | pubmed:meshHeading | pubmed-meshheading:21029756... | lld:pubmed |
| pubmed-article:21029756 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21029756 | pubmed:articleTitle | Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of ?-D-xylopyranose and ?-L-arabinofuranose. | lld:pubmed |
| pubmed-article:21029756 | pubmed:affiliation | Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84538 Bratislava, Slovakia. chempbsa@savba.sk | lld:pubmed |
| pubmed-article:21029756 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21029756 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
