Abstract
1. Isopenicillin N synthetase (IPNS) from Cephalosporium acremonium, which requires Fe2+ and O2 for activity, was highly purified for studies of factors affecting its conversion of delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine (LLD-ACV) into isopenicillin N (IPN). EDTA was used to quench the reaction by removal of Fe2+. 2. IPNS was inactivated during the course of the conversion of LLD-ACV into IPN, although it was relatively stable in the absence of LLD-ACV under otherwise similar conditions. In the presence of GSH and ascorbate each IPNS molecule carried out about 200 catalytic events before inactivation, but the turnover number was decreased 5-fold in the absence of ascorbate. 3. After trace metal ions had been removed from IPNS and other components of the reaction mixture by Chelex-100 resin, only about 10 microM-Fe2+ was required for maximum stimulation. Several other transition-metal ions were inhibitors of the enzyme. 4. Both dithiothreitol (DTT) and GSH stimulated IPNS activity, but GSH, unlike DTT, was not rapidly oxidized in the presence of O2 and Fe2+. 5. IPNS was rapidly inhibited by the thiol-blocking reagents N-ethylmaleimide and 2,2'- and 4,4'-dipyridyl disulphide, but not by 5,5'-dithiobis-(2-nitrobenzoic acid) in the same concentration. Inhibition by 2,2'-dipyridyl disulphide could be reversed by DTT.
MeSH Terms
Acremonium/enzymology
Cations, Divalent/pharmacology
Disulfides
Dithionitrobenzoic Acid/pharmacology
Dithiothreitol/pharmacology
Edetic Acid/pharmacology
Enzyme Inhibitors
Enzymes/metabolism
Ethylmaleimide/pharmacology
Ferrous Compounds/pharmacology
Glutathione/pharmacology
Oligopeptides/metabolism
Oxidoreductases
Pyridines/pharmacology
Chemicals
Cations, Divalent
Disulfides
Enzyme Inhibitors
Enzymes
Ferrous Compounds
Oligopeptides
Pyridines
5-(2-aminoadipyl)cysteinylvaline
4,4'-dipyridyl disulfide
ferrous sulfate
Dithionitrobenzoic Acid
Edetic Acid
Oxidoreductases
isopenicillin N synthetase
Glutathione
Ethylmaleimide
Dithiothreitol
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Perry D
Sir William Dunn School of Pathology, University of Oxford, U.K.
Abraham E P
Baldwin J E
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