1. L-leucine and its analogue: specific inhibitors for S-benzyl-L-cysteine-p-nitroanilide-hydrolyzing enzyme in Escherichia coli B
K Murata, Y Iba, Y Inoue, A Kimura Biochem Biophys Res Commun. 1988 Jun 16;153(2):767-72. doi: 10.1016/s0006-291x(88)81161-6.
An enzyme that catalyzes hydrolysis of S-benzyl-L-cysteine-p-nitroanilide was purified from E. coli B. The enzyme was a monomer with a molecular weight of 82,000. In addition to L-cysteinylglycine, the enzyme hydrolyzed various glycine-containing dipeptides most efficiently at pH 7.0. The enzyme required no metal ions for activity and was specifically inhibited by L-leucine and its analogue with free carboxyl group at the physiological concentrations.
