The roles of active site residues in the catalytic mechanism of methylaspartate ammonia-lyase☆

@inproceedings{Raj2013TheRO,
  title={The roles of active site residues in the catalytic mechanism of methylaspartate ammonia-lyase☆},
  author={Hans Gheyi Raj and Gerrit J Poelarends},
  booktitle={FEBS open bio},
  year={2013}
}
Methylaspartate ammonia-lyase (MAL; EC 4.3.1.2) catalyzes the reversible addition of ammonia to mesaconate to yield l-threo-(2S,3S)-3-methylaspartate and l-erythro-(2S,3R)-3-methylaspartate as products. In the proposed minimal mechanism for MAL of Clostridium tetanomorphum, Lys-331 acts as the (S)-specific base catalyst and abstracts the 3S-proton from l-threo-3-methylaspartate, resulting in an enolate anion intermediate. This enolic intermediate is stabilized by coordination to the essential… CONTINUE READING
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