Conserved sequence motifs in plant S-adenosyl-L-methionine-dependent methyltransferases

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 analys...

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Bibliographic Details
Published in:Plant molecular biology 1998-07, Vol.37 (4), p.663-674
Main Authors: Joshi, C.P. (Michigan Technological Univ., Houghton, MI (USA). School of Forestry and Wood Products), Chiang, V.L
Format: Article
Language:English
Subjects:
ACIDE AMINE
Amino Acid Sequence
AMINO ACIDS
AMINOACIDOS
Bacteria
Binding Sites - genetics
Biotechnology
Conserved Sequence
Enzymes
GENE
GENES
METABOLISM
METABOLISME
METABOLISMO
Methyltransferases - genetics
Methyltransferases - metabolism
Molecular Sequence Data
NUCLEOTIDE SEQUENCE
PLANTAS
PLANTE
PLANTS
Plants - enzymology
Plants - genetics
S-Adenosylmethionine - metabolism
SECUENCIA NUCLEOTIDICA
Sequence Homology, Amino Acid
SEQUENCE NUCLEOTIDIQUE
TRANSFERASAS
TRANSFERASE
TRANSFERASES
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Summary: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.
ISSN:0167-4412
1573-5028
DOI:10.1023/A:1006035210889