Reversible activation of aryl acylamidase from a coryneform bacterium, A-1, by a substrate, acetanilide

• Published in: Journal of Pesticide Science Vol. 18; no. 4; pp. 381 - 384
• Main Authors: MOCHIDA, K, NAKAMURA, T, WEN XIN LI, OZOE, Y
• Format: Journal Article
• Language: English
• Published: Tokyo Pesticide Science Society of Japan 1993; Japan Science and Technology Agency
• Subjects: Agronomy. Soil science and plant productions; Bacteriology; Biochemistry and biology; Biological and medical sciences; Chemical, physicochemical, biochemical and biological properties; Fundamental and applied biological sciences. Psychology; Metabolism. Enzymes; Microbiology; Physics, chemistry, biochemistry and biology of agricultural and forest soils; Soil science; Enzyme; Amidase; Activation; Reversible reaction; Metabolism; Substrate; Enzymatic activity; Bacteria; Hydrolases; Actinomycetes; Organic amide; Corynebacteriaceae; Nitrogen Organic compounds
• ISSN: 0385-1559; 1348-589X; 1349-0923
• DOI: 10.1584/jpestics.18.4_381

We have already reported that an aryl acylamidase produced extracellularly by a coryneform bacterium A-1 isolated from a paddy soil was markedly activated by preincubation with a substrate, acetanilide. The purified enzyme, having a molecular weight of 127,000, hydrolyzed not only acylanilides such as acetanilide, propanil and naproanilide but a phenylcarbamate chlorpropham and a phenylurea linuron. It is supposed that the activation mechanism might be explained in terms of the induced-fit of enzyme for acetanilide. The present study was conducted to elucidate the activation mechanism of aryl acylamidase by acetanilide.