Premium
Oxygen utilisation by isopenicillin n synthase from penicillium chrysogenum
Author(s) -
Bainbridge Zoë A.,
Scott Robert I.,
Perry David
Publication year - 1992
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280550306
Subject(s) - penicillium chrysogenum , oxygen , atp synthase , penicillium , chemistry , biochemistry , enzyme , organic chemistry , food science
The enzyme isopenicillin N synthase (IPNS) converts δ‐(L‐α‐aminoadipyl)‐L‐cysteinyl‐D‐valine (ACV) to isopenicillin N; an equimolar amount of oxygen is used in this oxidative ring closure reaction. Oxygen uptake rates of the reaction catalysed by partially purified IPNS from Penicillium chrysogenum SC 6140 and P2 were measured using an oxygen electrode. In contrast to published properties of Cephalosporium acremonium IPNS, the enzyme from P. chrysogenum was not stimulated by the addition of glutathione and showed reduced stimulation by Fe 2+ . The analysis of oxygen uptake rates showed the reaction to be first order with respect to oxygen concentration and the K m for ACV to be 0·4 mmol dm −3 . The implications of these results for cell‐free reactions using this enzyme and penicillin fermentations are discussed.