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Updated: Aug 14, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
delta-(D -alpha-Aminoadipoyl)-cleaving amidase of Ochrobactrum anthropi
1DECHEMA e.V., Biochemical Engineering, Karl-Winnacker-Institut, Theodor-Heuss-Allee 25, D-60486 Frankfurt/Main, Germany. patett@dechema.de
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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