PMID: 3142474Jul 1, 1988

Fumaraldehydic acid-induced inactivation of aspartase

Biochemistry International
Y HigashiM Tokushige

Abstract

Fumaraldehydic acid (FAA) induced a time-dependent inactivation of aspartase (L-aspartate ammonia-lyase, EC 4.3.1.1) from Escherichia coli at 30 degrees C and pH 7.4 following pseudo-first order kinetics. The rate of inactivation increased in proportion to the FAA concentration. In addition, the rate of inactivation increased, as the pH was increased. Determination of sulfhydryl groups showed that approximately one among 11 sulfhydryl groups was modified by FAA concomitant with the inactivation. L-Aspartate and fumarate protected the enzyme against FAA-inactivation, when Mg2+ ions were present. Unlike E. coli aspartase, P. fluorescens aspartase was not inactivated by FAA.

Related Concepts

Fumaraldehydic acid, (Z)-isomer
Ammonia-Lyases
Aspartate Ammonia-Lyase
Alkalescens-Dispar Group
Fatty Acids, Monounsaturated
Hydrogen-Ion Concentration
Pseudomonas fluorescens
Sulfhydryl Compounds

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