Isopenicillin N synthase: Difference between revisions
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<StructureSection load='1blz' size='400' side='right' scene='' caption='Isopenicilln N synthase complex with ACV and NO, [[1blz]]'> | |||
== Function == | == 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:10537113</ref>. | '''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:10537113</ref>. | ||
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== Structural highlights == | == 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<ref>PMID:9194566</ref>. | 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<ref>PMID:9194566</ref>. | ||
</StructureSection> | |||
==3D structures of isopenicillin N synthase== | ==3D structures of isopenicillin N synthase== | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
