Isopenicillin N synthase
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Revision as of 13:13, 30 December 2012
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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 synthase
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 - AnIPNS + ACV derivative
2jb4 - AnIPNS + cyclobutanone analog
1qje - AnIPNS + IPN + ACV
1blz - AnIPNS + NO + ACV
1obn, 1w04, 1w06 - AnIPNS + hydroxylamine + ACV derivative
Mn containing IPNS
1ips – AnIPNS