Computational insights into the mechanism of porphobilinogen synthase.

@article{Erdtman2010ComputationalII,
  title={Computational insights into the mechanism of porphobilinogen synthase.},
  author={Edvin Erdtman and Eric A. C. Bushnell and James W. Gauld and Leif A. Eriksson},
  journal={The journal of physical chemistry. B},
  year={2010},
  volume={114 50},
  pages={16860-70}
}
Porphobilinogen synthase (PBGS) is a key enzyme in heme biosynthesis that catalyzes the formation of porphobilinogen (PBG) from two 5-aminolevulinic acid (5-ALA) molecules via formation of intersubstrate C-N and C-C bonds. The active site consists of several invariant residues, including two lysyl residues (Lys210 and Lys263; yeast numbering) that bind the two substrate moieties as Schiff bases. Based on experimental studies, various reaction mechanisms have been proposed for this enzyme that… CONTINUE READING

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