Isopenicillin N synthase

Isopenicillin N synthase (IPNS) is an iron-dependent enzyme which catalyzes the formation of isopenicillin N (IPN) from the tripeptide aminoadipoyl-cysteine-valine (ACV). IPNS participates in the biosynthesis of penicillin and cephalosporin antibiotics. The active site of IPNS contains an Fe atom. The reaction involves the reduction of O2 molecule to H2O.

3D structures of isopenicillin N synthase3D structures of isopenicillin N synthase

Updated on 30-April-2015

{"openlevels":0}

• Fe containing IPNS
  • 1bk0 - AnIPNS + ACV – Aspergillus nidulans
    
  • 2bjs - AnIPNS (mutant) + ACV
    
  • 1qiq, 1qjf, 1hb1, 1hb2, 1hb3, 1hb4, 1odm, 1odn, 1oc1, 1uzw, 1w03, 1w05, 2bu9, 1w3v, 1w3x, 2ivi, 2ivj, 2vau, 2vbb, 2vbd, 2vbp, 2vcm, 2ve1, 2wo7, 2y6f, 2y60, 2y86, 4bb3 - AnIPNS + ACV derivative
    
  • 2jb4 - AnIPNS + cyclobutanone analog
    
  • 1qje - AnIPNS + IPN + ACV
    
  • 1blz - AnIPNS + NO + ACV
    
  • 1obn, 1w04, 1w06 - AnIPNS + hydroxylamine + ACV derivative
    
  • 3zku, 3zky, 3zoi, 4bb3 - IPNS + ACV derivative – Emericella nidulans
    
• Mn containing IPNS
  • 1ips – AnIPNS