Isopenicillin N synthase
From Proteopedia
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{{STRUCTURE_1blz| PDB=1blz | SIZE=400| SCENE= |right|CAPTION=Isopenicilln N synthase complex with ACV and NO, [[1blz]] }} | {{STRUCTURE_1blz| PDB=1blz | SIZE=400| SCENE= |right|CAPTION=Isopenicilln N synthase complex with ACV and NO, [[1blz]] }} | ||
| + | == 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<ref>PMID:9194566</ref>. | ||
| - | + | == Structural highlights == | |
==3D structures of isopenicillin N synthase== | ==3D structures of isopenicillin N synthase== | ||
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**[[1ips]] – AnIPNS | **[[1ips]] – AnIPNS | ||
}} | }} | ||
| + | == References == | ||
| + | <references/> | ||
[[Category: Topic Page]] | [[Category: Topic Page]] | ||
Revision as of 08:08, 3 April 2016
Contents |
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
3D structures of isopenicillin N synthase
Updated on 03-April-2016
References
- ↑ 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
