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: | Baldwin, J, Adlington, R, Coates, J, Crabbe, M, Crouch, N, Keeping, J, Knight, G, Schofield, C, Ting, H, Vallejo, C |
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Format: | Journal article |
Sprog: | English |
Udgivet: |
1987
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Lignende værker
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Substrate specificity of cloned deacetoxycephalosporin C/deacetylcephalosporin C synthetase.
af: Baldwin, J, et al.
Udgivet: (1988) -
STEPWISE HYDROGEN REMOVAL IN THE ENZYMATIC RING EXPANSION OF PENICILLIN-N TO DEACETOXYCEPHALOSPORIN-C
af: Baldwin, J, et al.
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Oxidation of deacetylcephalosporin C by deacetoxycephalosporin C/deacetylcephalosporin C synthase.
af: Baldwin, J, et al.
Udgivet: (1992) -
Controlling the substrate selectivity of deacetoxycephalosporin/deacetylcephalosporin C synthase.
af: Lloyd, MD, et al.
Udgivet: (2004) -
ENZYMATIC RING EXPANSION OF PENICILLINS TO CEPHALOSPORINS - SIDE-CHAIN SPECIFICITY
af: Baldwin, J, et al.
Udgivet: (1987)