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J Bacteriol. 1971 November; 108(2): 809-816
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Amino Acid-ß-Naphthylamide Hydrolysis by Pseudomonas aeruginosa Arylamidase

Department of Microbiology, Medical College of Georgia, Augusta, Georgia 30902

ABSTRACT

The intracellular and constitutive arylamidase from Pseudomonas aeruginosa was purified 528-fold by salt fractionation, ion-exchange chromatography, gel filtration, and adsorption chromatography. This enzyme hydrolyzed basic and neutral N-terminal amino acid residues from amino-ß-naphthylamides, dipeptide-ß-naphthylamides, and a variety of polypeptides. Only those substrates having an L-amino acid with an unsubstituted -amino group as the N-terminal residue were susceptible to enzymatic hydrolysis. The molecular weight was estimated to be 71,000 daltons. The lowest K_m values were associated with substrates having neutral or basic amino acid residues with large side chains with no substitution or branching on the ß carbon atom.