Alliin Lyase from Garlic, Allium sativum: Investigations on Enzyme/Substrate, Enzyme/Inhibitor Interactions, and on a New Coenzyme

Abstract

A purified alliin lyase (EC 4.4.1.4) from garlic (Allium sativum L.) has been characterized by kinetic and spectral data under the addition of different substrates, inhibitors, and reducing agents. Hydroxylamine sulfate (50 µM) inhibited the alliinase activity by nearly 90%. Rotenone revealed a similar effect at a concentration of 10 nano-molar. Examination of L-cysteine, and a series of related compounds, on a competitive inhibitory effect on the alliinase-catalyzed alliin cleavage resulted in a list of essential functional groups for substances with this property. Spectral studies on the purified, yellow appearing alliinase enzyme confirmed the existance of an unknown flavinecoenzyme.