| pubmed-article:17031032 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17031032 | lifeskim:mentions | umls-concept:C0446085 | lld:lifeskim |
| pubmed-article:17031032 | lifeskim:mentions | umls-concept:C0028959 | lld:lifeskim |
| pubmed-article:17031032 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:17031032 | lifeskim:mentions | umls-concept:C0117605 | lld:lifeskim |
| pubmed-article:17031032 | lifeskim:mentions | umls-concept:C0597571 | lld:lifeskim |
| pubmed-article:17031032 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:17031032 | pubmed:dateCreated | 2006-10-23 | lld:pubmed |
| pubmed-article:17031032 | pubmed:abstractText | A unique N-linked glycosylation motif (Asn(79)-Tyr-Thr) was found in the sequence of type-A feruloyl esterases from Aspergillus spp. To clarify the function of the flap, the role of N-linked oligosaccharides located in the flap region on the biochemical properties of feruloyl esterase (AwFAEA) from Aspergillus awamori expressed in Pichia pastoris was analyzed by removing the N-linked glycosylation recognition site by site-directed mutagenesis. N79 was replaced with A or Q. N-glycosylation-free N79A and N79Q mutant enzymes had lower activity than that of the glycosylated recombinant AwFAEA wild-type enzyme toward alpha-naphthylbutyrate (C4), alpha-naphthylcaprylate (C8), and phenolic acid methyl esters. Kinetic analysis of the mutant enzymes indicated that the lower catalytic efficiency was due to a combination of increased Km and decreased k(cat) for N79A, and to a considerably decreased k(cat) for N79Q. N79A and N79Q mutant enzymes also exhibited considerably reduced thermostability relative to the wild-type. | lld:pubmed |
| pubmed-article:17031032 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17031032 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17031032 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17031032 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17031032 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17031032 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17031032 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17031032 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17031032 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17031032 | pubmed:issn | 0916-8451 | lld:pubmed |
| pubmed-article:17031032 | pubmed:author | pubmed-author:TakahashiKenj... | lld:pubmed |
| pubmed-article:17031032 | pubmed:author | pubmed-author:FushinobuShin... | lld:pubmed |
| pubmed-article:17031032 | pubmed:author | pubmed-author:KosekiTakuyaT | lld:pubmed |
| pubmed-article:17031032 | pubmed:author | pubmed-author:HashizumeKats... | lld:pubmed |
| pubmed-article:17031032 | pubmed:author | pubmed-author:YamaneYuichiY | lld:pubmed |
| pubmed-article:17031032 | pubmed:author | pubmed-author:HandaTakashiT | lld:pubmed |
| pubmed-article:17031032 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17031032 | pubmed:volume | 70 | lld:pubmed |
| pubmed-article:17031032 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17031032 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17031032 | pubmed:pagination | 2476-80 | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:meshHeading | pubmed-meshheading:17031032... | lld:pubmed |
| pubmed-article:17031032 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17031032 | pubmed:articleTitle | N-linked oligosaccharides of Aspergillus awamori feruloyl esterase are important for thermostability and catalysis. | lld:pubmed |
| pubmed-article:17031032 | pubmed:affiliation | National Research Institute of Brewing, Japan. tkoseki@tds1.tr.yamagata-u.ac.jp | lld:pubmed |
| pubmed-article:17031032 | pubmed:publicationType | Journal Article | lld:pubmed |
