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. 1971 Nov;108(2):809–816. doi: 10.1128/jb.108.2.809-816.1971

Amino Acid-β-Naphthylamide Hydrolysis by Pseudomonas aeruginosa Arylamidase

P S Riley 1, Francis J Behal 1
PMCID: PMC247145  PMID: 5001871

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-β-naphthylamides, dipeptide-β-naphthylamides, and a variety of polypeptides. Only those substrates having an l-amino acid with an unsubstituted α-amino group as the N-terminal residue were susceptible to enzymatic hydrolysis. The molecular weight was estimated to be 71,000 daltons. The lowest Km values were associated with substrates having neutral or basic amino acid residues with large side chains with no substitution or branching on the β carbon atom.

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Selected References

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