A novel aminopeptidase was purified by high performance liquid chromatography from a cytosoluble 100000 g extract of on the basis of its ability to cleave L-arginine 7-amino-4-methylcoumarin. The purification factor was 36 and the yield was 20%. The native enzyme had a mol. wt of 52 kDa as demonstrated by SDS-PAGE in the presence or absence of reducing conditions and exhibited an iso-electric point of 4·3. The aminopeptidase showed optimum activity at pH 7·2, a Michaelis constant of c. 50 μM and a V at 19 mM AMC released/min/mg of protein for L-Arg-AMC. This enzyme was shown to cleave at low affinity L-leucine-7-amino-4-methylcoumarin as demonstrated by the spectrofluorimetric method. The enzyme was strongly inhibited by specific metallo-enzyme inhibitors—EDTA and o-phenanthroline. Furthermore, there is evidence that a similar or identical enzyme occurs in other clinical isolates and other spp.


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