Function
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[1].
Structural highlights
IPNS active site contains Fe+2 and the substrate ACV. The Fe+2 ion is hexacoordinated to 3 IPNS side chains, one water molecule, the ACV thiolate moiety and NO[2]. Water molecules shown as red spheres.
- ↑ Burzlaff NI, Rutledge PJ, Clifton IJ, Hensgens CM, Pickford M, Adlington RM, Roach PL, Baldwin JE. The reaction cycle of isopenicillin N synthase observed by X-ray diffraction. Nature. 1999 Oct 14;401(6754):721-4. PMID:10537113 doi:10.1038/44400
- ↑ Roach PL, Clifton IJ, Hensgens CM, Shibata N, Schofield CJ, Hajdu J, Baldwin JE. Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation. Nature. 1997 Jun 19;387(6635):827-30. PMID:9194566 doi:https://dx.doi.org/10.1038/42990
