Isopenicillin N synthase

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Contents 1 Function 2 Structural highlights 3 3D structures of isopenicillin N synthase 4 References

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 pentacoordinated to 3 IPNS side chains, one water molecule and the ACV thiolate moiety^[2].

3D structures of isopenicillin N synthase

Updated on 03-April-2016

References

1. ↑ 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
2. ↑ 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:http://dx.doi.org/10.1038/42990