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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2004-11-23
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
577
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
367-70
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15556611-Acyl Coenzyme A,
pubmed-meshheading:15556611-Amino Acid Sequence,
pubmed-meshheading:15556611-Ammi,
pubmed-meshheading:15556611-Animals,
pubmed-meshheading:15556611-Cations, Divalent,
pubmed-meshheading:15556611-Cells, Cultured,
pubmed-meshheading:15556611-Cloning, Molecular,
pubmed-meshheading:15556611-Cobalt,
pubmed-meshheading:15556611-Conserved Sequence,
pubmed-meshheading:15556611-Escherichia coli,
pubmed-meshheading:15556611-Kinetics,
pubmed-meshheading:15556611-Magnesium,
pubmed-meshheading:15556611-Manganese,
pubmed-meshheading:15556611-Methyltransferases,
pubmed-meshheading:15556611-Molecular Structure,
pubmed-meshheading:15556611-Molecular Weight,
pubmed-meshheading:15556611-Mutation,
pubmed-meshheading:15556611-Quercetin,
pubmed-meshheading:15556611-Recombinant Proteins,
pubmed-meshheading:15556611-Sequence Homology, Amino Acid,
pubmed-meshheading:15556611-Substrate Specificity
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pubmed:year |
2004
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pubmed:articleTitle |
Cations modulate the substrate specificity of bifunctional class I O-methyltransferase from Ammi majus.
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pubmed:affiliation |
Institut für Pharmazeutische Biologie der Philipps-Universität Marburg, Deutschhausstr. 17A, D- 35037 Marburg/Lahn, Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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