The crystal structure of isopenicillin N synthase with δ-(l-α-aminoadipoyl)-l-cysteinyl-d-methionine reveals thioether coordination to iron

Publication year: 2011 Source: Archives of Biochemistry and Biophysics, Available online 6 October 2011 Ian J. Clifton, Ge Wei, Robert M. Adlington, Jack E. Baldwin, Peter J. Rutledge Isopenicillin N synthase (IPNS) catalyses cyclisation of -l–aminoadipoyl-l-cysteinyl-d-valine (ACV) to isopenicillin N (IPN), the central step in penicillin biosynthesis. Previous studies have shown that IPNS turns over a wide range of substrate analogues in which the valine residue of its natural substrate is replaced with other amino acids. IPNS accepts and oxidizes numerous substrates that bear hydrocarbon sidechains in this position, however the enzyme is less tolerant of analogues presenting polar functionality in place of the valinyl isopropyl group

Publication year: 2011 Source: Archives of Biochemistry and Biophysics, Available online 6 October 2011 Ian J. Clifton, Ge Wei, Robert M. Adlington, Jack E. Baldwin, Peter J. Rutledge Isopenicillin N synthase (IPNS) catalyses cyclisation of -l–aminoadipoyl-l-cysteinyl-d-valine (ACV) to isopenicillin N (IPN), the central step in penicillin biosynthesis. Previous studies have shown that IPNS turns over a wide range of substrate analogues in which the valine residue of its natural substrate is replaced with other amino acids. IPNS accepts and oxidizes numerous substrates that bear hydrocarbon sidechains in this position, however the enzyme is less tolerant of analogues presenting polar functionality in place of the valinyl isopropyl group

See the original article here:
The crystal structure of isopenicillin N synthase with δ-(l-α-aminoadipoyl)-l-cysteinyl-d-methionine reveals thioether coordination to iron

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