The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)- Malyl-CoA thioesterase.

@article{Erb2010TheAM,
  title={The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/\{beta\}-methylmalyl-CoA lyase and (3S)- Malyl-CoA thioesterase.},
  author={Tobias J Erb and Lena Frerichs-Revermann and Georg Fuchs and Birgit E. Alber},
  journal={Journal of bacteriology},
  year={2010},
  volume={192 5},
  pages={1249-58}
}
Assimilation of acetyl coenzyme A (acetyl-CoA) is an essential process in many bacteria that proceeds via the glyoxylate cycle or the ethylmalonyl-CoA pathway. In both assimilation strategies, one of the final products is malate that is formed by the condensation of acetyl-CoA with glyoxylate. In the glyoxylate cycle this reaction is catalyzed by malate synthase, whereas in the ethylmalonyl-CoA pathway the reaction is separated into two proteins: malyl-CoA lyase, a well-known enzyme catalyzing… CONTINUE READING