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. 1973 Nov;26(5):709-18.
doi: 10.1128/am.26.5.709-718.1973.

Purification and properties of an aryl acylamidase of Bacillus sphaericus, catalyzing the hydrolysis of various phenylamide herbicides and fungicides

G Engelhardt, P R Wallnöfer, R Plapp

Purification and properties of an aryl acylamidase of Bacillus sphaericus, catalyzing the hydrolysis of various phenylamide herbicides and fungicides

G Engelhardt et al. Appl Microbiol. 1973 Nov.

Abstract

From Bacillus sphaericus ATCC 12123 an aryl acylamidase (EC 3.5.1.13) was purified to homogeneity by ion exchange chromatography, gel filtration, and polyacrylamide gel electrophoresis. The enzyme is inducible by various phenylamides of the acylanilide, phenylcarbamate, and methoxysubstituted phenylurea type. It has a molecular weight of 75,000. Enzyme activity was inhibited by sulfhydryl reagents, several metal ions, and 3,4-dichloroaniline (a product of linuron degradation). A requirement for divalent metal ions in enzyme activity could not be demonstrated. In the presence of 6 M urea an irreversible inactivation of the enzyme occurred. The hydrolysis of L-alanine-4-nitroanilide was competitively inhibited by puromycin.

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