Collect. Czech. Chem. Commun. 1992, 57, 2181-2186

Substrate Specificity of Carboxylesterase from Vicia faba Roots

Jana Barthováa, Hana Löfellmannováa and Karel Benešb

a Department of Biochemistry, Charles University, 128 40 Prague 2
b Institute of Molecular Biology of Plants, Czechoslovak Academy of Sciences, 370 05 České Budějovice


Michaelis constants values and limiting rates of the reaction catalyzed by carboxylesterase isolated from the root tips of Vicia faba were determined. 1-Naphthyl acetate, 1-naphthyl butyrate, 1-naphthyl ester of N-acetylglycine, 1-naphthyl ester of L-leucine and 1-naphthyl ester of N-acetyl-L-leucine were used as substrates. The values for the enzyme from control plants were compared with the data for carboxylesterase from plants exposed to the effect of 2,4-dichlorophenoxyacetic acid. An electrophoretic analysis of enzymes from control plants and the tested plants was carried out.