Purification and initial characterization of an enzyme with deacetoxycephalosporin C synthetase and hydroxylase activities.
Deacetoxycephalosporin C synthetase (expandase) from Cephalosporium acremonium (Acremonium chrysogenum) was purified to near homogeneity as judged by SDS/polyacrylamide-gel electrophoresis. The enzyme (Mr about 40,000) exhibited a pH optimum around 7.5. It required 2-oxoglutarate (Km 0.04 mM), Fe2+...
Main Authors: | , , , , , , , , , |
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Format: | Journal article |
Language: | English |
Published: |
1987
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