Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism.

@article{Gonzlez2003CrystalSO,
  title={Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism.},
  author={Beatriz Gonz{\'a}lez and Mar{\'i}a Angeles Pajares and Juan A Hermoso and Danielle Guillerm and Georges Guillerm and Julia Sanz-Aparicio},
  journal={Journal of molecular biology},
  year={2003},
  volume={331 2},
  pages={407-16}
}
Methionine adenosyltransferases (MATs) are a family of enzymes in charge of synthesising S-adenosylmethionine (SAM), the most important methyl donor present in living organisms. These enzymes use methionine and ATP as reaction substrates, which react in a S(N)2 fashion where the sulphur atom from methionine attacks C5' from ATP while triphosphate chain is cleaved. A MAT liver specific isoenzyme has been detected, which exists in two distinct oligomeric forms, a dimer (MAT III) and a tetramer… CONTINUE READING

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