A novel methyltransferase catalyzes the methyl esterification of trans-aconitate in Escherichia coli.

@article{Cai1999ANM,
  title={A novel methyltransferase catalyzes the methyl esterification of trans-aconitate in Escherichia coli.},
  author={Hui Cai and Steven G. Clarke},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 19},
  pages={
          13470-9
        }
}
We have identified a new type of S-adenosyl-L-methionine-dependent methyltransferase in the cytosol of Escherichia coli that is expressed in early stationary phase under the control of the RpoS sigma factor. This enzyme catalyzes the monomethyl esterification of trans-aconitate at high affinity (Km = 0.32 mM) and cis-aconitate, isocitrate, and citrate at lower velocities and affinities. We have purified the enzyme to homogeneity by gel-filtration, anion-exchange, and hydrophobic chromatography… CONTINUE READING

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