Functional and structural characterization of a cation-dependent O-methyltransferase from the cyanobacterium Synechocystis sp. strain PCC 6803.

@article{Kopycki2008FunctionalAS,
  title={Functional and structural characterization of a cation-dependent O-methyltransferase from the cyanobacterium Synechocystis sp. strain PCC 6803.},
  author={Jakub Grzegorz Kopycki and Milton T Stubbs and Wolfgang Brandt and M. Hagemann and Andrea Porzel and J{\"u}rgen G. Schmidt and Willibald Schliemann and Meinhart H. Zenk and Thomas Joesf Vogt},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 30},
  pages={
          20888-96
        }
}
The coding sequence of the cyanobacterium Synechocystis sp. strain PCC 6803 slr0095 gene was cloned and functionally expressed in Escherichia coli. The corresponding enzyme was classified as a cation- and S-adenosyl-l-methionine-dependent O-methyltransferase (SynOMT), consistent with considerable amino acid sequence identities to eukaryotic O-methyltransferases (OMTs). The substrate specificity of SynOMT was similar with those of plant and mammalian CCoAOMT-like proteins accepting a variety of… CONTINUE READING

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