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+...
Prif Awduron: | Baldwin, J, Adlington, R, Coates, J, Crabbe, M, Crouch, N, Keeping, J, Knight, G, Schofield, C, Ting, H, Vallejo, C |
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Fformat: | Journal article |
Iaith: | English |
Cyhoeddwyd: |
1987
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Eitemau Tebyg
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Substrate specificity of cloned deacetoxycephalosporin C/deacetylcephalosporin C synthetase.
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STEPWISE HYDROGEN REMOVAL IN THE ENZYMATIC RING EXPANSION OF PENICILLIN-N TO DEACETOXYCEPHALOSPORIN-C
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Oxidation of deacetylcephalosporin C by deacetoxycephalosporin C/deacetylcephalosporin C synthase.
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Controlling the substrate selectivity of deacetoxycephalosporin/deacetylcephalosporin C synthase.
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ENZYMATIC RING EXPANSION OF PENICILLINS TO CEPHALOSPORINS - SIDE-CHAIN SPECIFICITY
gan: Baldwin, J, et al.
Cyhoeddwyd: (1987)