| pubmed-article:15556611 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15556611 | lifeskim:mentions | umls-concept:C0331050 | lld:lifeskim |
| pubmed-article:15556611 | lifeskim:mentions | umls-concept:C0007447 | lld:lifeskim |
| pubmed-article:15556611 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
| pubmed-article:15556611 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:15556611 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:15556611 | pubmed:dateCreated | 2004-11-23 | lld:pubmed |
| pubmed-article:15556611 | pubmed:abstractText | Caffeoyl-coenzyme A O-methyltransferase cDNA was cloned from dark-grown Ammi majus L. (Apiaceae) cells treated with a crude fungal elicitor and the open reading frame was expressed in Escherichia coli. The translated polypeptide of 27.1-kDa shared significant identity to other members of this highly conserved class of proteins and was 98.8% identical to the corresponding O-methyltransferase from parsley. For biochemical characterization, the recombinant enzyme could be purified to apparent homogeneity by metal-affinity chromatography, although the recombinant enzyme did not contain any affinity tag. Based on sequence analysis and substrate specificity, the enzyme classifies as a cation-dependent O-methyltransferase with pronounced preference for caffeoyl coenzyme A, when assayed in the presence of Mg2+-ions. Surprisingly, however, the substrate specificity changed dramatically, when Mg2+ was replaced by Mn2+ or Co2+ in the assays. This effect could point to yet unknown functions and substrate specificities in situ and suggests promiscuous roles for the lignin specific cluster of plant O-methyltransferases. | lld:pubmed |
| pubmed-article:15556611 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15556611 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15556611 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15556611 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15556611 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15556611 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15556611 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15556611 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15556611 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15556611 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15556611 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15556611 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15556611 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15556611 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:15556611 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:15556611 | pubmed:author | pubmed-author:VogtThomasT | lld:pubmed |
| pubmed-article:15556611 | pubmed:author | pubmed-author:LukacinRichar... | lld:pubmed |
| pubmed-article:15556611 | pubmed:author | pubmed-author:MaternUlrichU | lld:pubmed |
| pubmed-article:15556611 | pubmed:author | pubmed-author:SpeckerSilvia... | lld:pubmed |
| pubmed-article:15556611 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15556611 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:15556611 | pubmed:volume | 577 | lld:pubmed |
| pubmed-article:15556611 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15556611 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15556611 | pubmed:pagination | 367-70 | lld:pubmed |
| pubmed-article:15556611 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15556611 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15556611 | pubmed:articleTitle | Cations modulate the substrate specificity of bifunctional class I O-methyltransferase from Ammi majus. | lld:pubmed |
| pubmed-article:15556611 | pubmed:affiliation | Institut für Pharmazeutische Biologie der Philipps-Universität Marburg, Deutschhausstr. 17A, D- 35037 Marburg/Lahn, Germany. | lld:pubmed |
| pubmed-article:15556611 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15556611 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15556611 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15556611 | lld:pubmed |
