1887

Abstract

The isopenicillin N synthase (cyclase) of (syn. ) has been purified to near homogeneity as judged by SDS-PAGE and isoelectric focusing. This enzyme catalyses the oxidative cyclization of the tripeptide -(-α-aminoadipyl)--cysteinyl--valine to isopenicillin N. The enzyme required DTT, Fe and oxygen and it was greatly stimulated by ascorbic acid. It was strongly inhibited by Co, Zn and Mn. Optimal pH and temperature were 7·0 and 25 °C (with the assay conditions used), respectively. The apparent of isopenicillin N synthase for -(-α-aminoadipyl)--cysteinyl--valine was 0·18 m. The enzyme is a monomer with an of 26500 ± 1000 and a pI of 6.55.

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1988-01-01
2021-07-27
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