delta-(D -alpha-Aminoadipoyl)-cleaving amidase of Ochrobactrum anthropi.
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.
Patett
F
F
DECHEMA e.V., Biochemical Engineering, Karl-Winnacker-Institut, Theodor-Heuss-Allee 25, D-60486 Frankfurt/Main, Germany. patett@dechema.de
Fischer
L
L
D015074:2-Aminoadipic Acid / Q000737:chemistry / Q000378:metabolism*; D000581:Amidohydrolases / Q000378:metabolism*; D001673:Biodegradation, Environmental; D002455:Cell Division / Q000187:drug effects; D002458:Cell Fractionation; D002462:Cell Membrane / Q000378:metabolism; D002511:Cephalosporins / Q000737:chemistry; D003374:Coumarins / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D017672:Nitrogen Compounds / Q000494:pharmacology; D020621:Ochrobactrum anthropi / Q000166:cytology / Q000201:enzymology* / Q000302:isolation & purification; D011503:Transglutaminases / Q000378:metabolism
D002511:Cephalosporins; D003374:Coumarins; D017672:Nitrogen Compounds; D015074:2-Aminoadipic Acid; C025163:cephalosporin C; D011503:Transglutaminases; D000581:Amidohydrolases; C028743:7-amino-4-methylcoumarin