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A coupled enzyme assay for isopenicillin N synthetase

✍ Scribed by Jack E. Baldwin; Simon E. Moroney; Hong-Hoi Ting

Publisher
Elsevier Science
Year
1985
Tongue
English
Weight
327 KB
Volume
145
Category
Article
ISSN
0003-2697

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✦ Synopsis

The development of a coupled enzyme assay for the determination of isopenicilhn N synthetase activity in purified extracts from Cephalosporium acremonium was described. Isopenicillin N formed from its precursor, 8-(t-cr-aminoadipyl)-t-cysteinyl-o-valine (ACV), by the synthetase was hydrolyzed by @-lactamase I to the corresponding penicilloic acid. Automatic titration of the acid with standard sodium hydroxide delivered by a pH-stat gave a continuous plot of product formed vs time. This assay has been used in kinetic studies and to determine the effects of pH, ionic strength, and temperature on the enzyme's activity.

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