| pubmed-article:21038099 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21038099 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:21038099 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:21038099 | pubmed:dateCreated | 2011-2-10 | lld:pubmed |
| pubmed-article:21038099 | pubmed:abstractText | Recently, the prenyltransferase SirD was found to be responsible for the O-prenylation of tyrosine in the biosynthesis of sirodesmin PL in Leptosphaeria maculans. In this study, the behavior of SirD towards phenylalanine/tyrosine and tryptophan derivatives was investigated. Product formation has been observed with 12 of 19 phenylalanine/tyrosine derivatives. It was shown that the alanine structure attached to the benzene ring and an electron donor, e.g., OH or NH?, at its para-position are essential for the enzyme activity. Modifications were possible both at the side chain and the benzene ring. Enzyme products from seven phenylalanine/tyrosine derivatives were isolated and characterized by MS and NMR analyses including HSQC and HMBC and proven to be O- or N-prenylated derivatives at position C4 of the benzene rings. K ( M ) values of six selected derivatives were found in the range of 0.10-0.68 mM. Catalytic efficiencies (K(cat)/K(M)) were determined in the range of 430-1,110 s?¹·M?¹ with L-tyrosine as the best substrate. In addition, 7 of 14 tested tryptophan analogs were also accepted by SirD and converted to C7-prenylated derivatives, which was confirmed by comparison with products obtained from enzyme assays using a 7-dimethylallyltryptophan synthase 7-DMATS from Aspergillus fumigatus. | lld:pubmed |
| pubmed-article:21038099 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21038099 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21038099 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21038099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21038099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21038099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21038099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21038099 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21038099 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:21038099 | pubmed:issn | 1432-0614 | lld:pubmed |
| pubmed-article:21038099 | pubmed:author | pubmed-author:LiShu-MingSM | lld:pubmed |
| pubmed-article:21038099 | pubmed:author | pubmed-author:XieXiulanX | lld:pubmed |
| pubmed-article:21038099 | pubmed:author | pubmed-author:ZhengXiao-Don... | lld:pubmed |
| pubmed-article:21038099 | pubmed:author | pubmed-author:ZouHui-XiHX | lld:pubmed |
| pubmed-article:21038099 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21038099 | pubmed:volume | 89 | lld:pubmed |
| pubmed-article:21038099 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21038099 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21038099 | pubmed:pagination | 1443-51 | lld:pubmed |
| pubmed-article:21038099 | pubmed:meshHeading | pubmed-meshheading:21038099... | lld:pubmed |
| pubmed-article:21038099 | pubmed:meshHeading | pubmed-meshheading:21038099... | lld:pubmed |
| pubmed-article:21038099 | pubmed:meshHeading | pubmed-meshheading:21038099... | lld:pubmed |
| pubmed-article:21038099 | pubmed:meshHeading | pubmed-meshheading:21038099... | lld:pubmed |
| pubmed-article:21038099 | pubmed:meshHeading | pubmed-meshheading:21038099... | lld:pubmed |
| pubmed-article:21038099 | pubmed:meshHeading | pubmed-meshheading:21038099... | lld:pubmed |
| pubmed-article:21038099 | pubmed:meshHeading | pubmed-meshheading:21038099... | lld:pubmed |
| pubmed-article:21038099 | pubmed:meshHeading | pubmed-meshheading:21038099... | lld:pubmed |
| pubmed-article:21038099 | pubmed:meshHeading | pubmed-meshheading:21038099... | lld:pubmed |
| pubmed-article:21038099 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21038099 | pubmed:articleTitle | The tyrosine O-prenyltransferase SirD catalyzes O-, N-, and C-prenylations. | lld:pubmed |
| pubmed-article:21038099 | pubmed:affiliation | Department of Food Science and Nutrition, Zhejiang University, 310029 Hangzhou, Zhejiang, People's Republic of China. | lld:pubmed |
| pubmed-article:21038099 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21038099 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
