Abstract
A hydroxylase catalysing the conversion of anthranilic acid to 3-hydroxy-anthranilic acid has been isolated from the leaves of Tecoma stans . The enzyme was purified by fractional precipitation with acetone and adsorption on DEAE-cellulose to give about 84-fold increase in specific activity. The optimum pH for the reaction was 5.0. Among the compounds tested, only anthranilic acid was effective as substrate. The enzyme was inhibited by concentrations of anthranilic acid above 1 mM. Metal-chelating agents and sulfhydryl compounds produced marked inhibition. The enzyme was activated by Fe 3+ and the inhibition with α-α ′-dipyridyl was specifically reversed by Fe 3+ . The enzyme showed an absolute requirement for tetrahydrofolic acid and reduced nicotinamide coenzymes for activity.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
