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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1998-8-10
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pubmed:abstractText |
Plant S-adenosyl-L-methionine-dependent methyltransferases (SAM-Mtases) are the key enzymes in phenylpropanoid, flavonoid and many other metabolic pathways of biotechnological importance. Here we compiled the amino acid sequences of 56 SAM-Mtases from different plants and performed a computer analysis for the conserved sequence motifs that could possibly act as SAM-binding domains. To date, genes or cDNAs encoding at least ten distinct groups of SAM-Mtases that utilize SAM and a variety of substrates have been reported from higher plants. Three amino acid sequence motifs are conserved in most of these SAM-Mtases. In addition, many conserved domains have been discovered in each group of O-methyltransferases (OMTs) that methylate specific substrates and may act as sites for substrate specificity in each enzyme. Finally, a diagrammatic representation of the relationship between different OMTs is presented. These SAM-Mtase sequence signatures will be useful in the identification of SAM-Mtase motifs in the hitherto unidentified proteins as well as for designing primers in the isolation of new SAM-Mtases from plants.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
0167-4412
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
37
|
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
663-74
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9687070-Amino Acid Sequence,
pubmed-meshheading:9687070-Binding Sites,
pubmed-meshheading:9687070-Conserved Sequence,
pubmed-meshheading:9687070-Methyltransferases,
pubmed-meshheading:9687070-Molecular Sequence Data,
pubmed-meshheading:9687070-Plants,
pubmed-meshheading:9687070-S-Adenosylmethionine,
pubmed-meshheading:9687070-Sequence Homology, Amino Acid
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pubmed:year |
1998
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pubmed:articleTitle |
Conserved sequence motifs in plant S-adenosyl-L-methionine-dependent methyltransferases.
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pubmed:affiliation |
Plant Biotechnology Research Center, Institute of Wood Research, School of Forestry and Wood Products, Michigan Technological University, Houghton 49931, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|