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

Plant Mol Biol. 1998 Jul;37(4):663-74. doi: 10.1023/a:1006035210889.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites / genetics
  • Conserved Sequence*
  • Methyltransferases / genetics*
  • Methyltransferases / metabolism
  • Molecular Sequence Data
  • Plants / enzymology*
  • Plants / genetics*
  • S-Adenosylmethionine / metabolism
  • Sequence Homology, Amino Acid

Substances

  • S-Adenosylmethionine
  • Methyltransferases