Abstract
Ochrobactrum anthropi cleaved the delta-(D-alpha-aminoadipoyl)-side chain from delta-(D-alpha-aminoadipoyl)-7-amino-4-methylcoumarin, a beta-lactamase-resistant cephalosporin C analogue. In whole cell conversions up to 1 nkat g(-1) dry cell wt were achieved. O. anthropi possesses also gamma-D-glutamyltranspeptidase activity, 8 nkat g(-1) dry cell wt, the likely cause of delta-(D-alpha-aminoadipoyl)-cleavage.
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