Oxygen utilisation by isopenicillin n synthase from penicillium chrysogenum
- 1 January 1992
- journal article
- research article
- Published by Wiley in Journal of Chemical Technology & Biotechnology
- Vol. 55 (3) , 233-238
- https://doi.org/10.1002/jctb.280550306
Abstract
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 Fe2+. The analysis of oxygen uptake rates showed the reaction to be first order with respect to oxygen concentration and the Km 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.Keywords
This publication has 18 references indexed in Scilit:
- The biosynthesis of penicillins and cephalosporinsNatural Product Reports, 1988
- 4536476 Stable epimerase reagent, cyclase reagent and ring expansion reagent for cell-free production of cephalosporins: Saul Wolfe, Donal Westlake, Susan Jensen, Kingston, Canada assigned to Queen's University at KingstonBiotechnology Advances, 1986
- Purification of isopenicillin N synthetase from Streptomyces clavuligerusCanadian Journal of Microbiology, 1986
- Cloning and expression of the isopenicillin N synthetase gene from Penicillium chrysogenumGene, 1986
- Isolation, sequence determination and expression in Escherichia coli of the isopenicillin N synthetase gene from Cephalosporium acremoniumNature, 1985
- Isopenicillin N synthetase of Penicillium chrysogenum, an enzyme that converts delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine to isopenicillin NAntimicrobial Agents and Chemotherapy, 1985
- Bacterial cytochrome oxidases a structurally and functionally diverse group of electron-transfer proteinBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1983
- Studies on the ring-cyclization and ring-expansion enzymes of β-lactam biosynthesis in Cephalosporium acremoniumCanadian Journal of Microbiology, 1983
- Cell-free cyclization of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine to isopenicillin NAntimicrobial Agents and Chemotherapy, 1980
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976