Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes

@article{Roach1995CrystalSO,
  title={Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes},
  author={Peter L Roach and Ian J. Clifton and Vilmos F{\"u}l{\"o}p and Karl Harlos and Geoffrey J. Barton and J{\'a}nos Hajdu and Inger Andersson and Christopher J. Schofield and Jack E. Baldwin},
  journal={Nature},
  year={1995},
  volume={375},
  pages={700-704}
}
PENICILLIN antibiotics are all produced from fermentation-derived penicillins because their chemical synthesis is not commercially viable. The key step in penicillin biosynthesis, in which both the β-lactam and thiazolidine rings of the nucleus are created, is mediated by isopenicillin N synthase (IPNS), which binds ferrous iron and uses dioxygen as a cosubstrate. In a unique enzymatic step, with no chemical precedent, IPNS catalyses the transfer of four hydrogen atoms from its tripeptide… CONTINUE READING

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