TY - JOUR
T1 - L-leucine and its analogue
T2 - Specific inhibitors for S-benzyl-L-cysteine-p-nitroanilide-hydrolyzing enzyme in Escherichia coli B
AU - Murata, Kousaku
AU - Iba, Yoshitaka
AU - Inoue, Yoshiharu
AU - Kimura, Akira
PY - 1988/6/16
Y1 - 1988/6/16
N2 - 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.
AB - 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.
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U2 - 10.1016/S0006-291X(88)81161-6
DO - 10.1016/S0006-291X(88)81161-6
M3 - Article
C2 - 3289539
AN - SCOPUS:0024289943
SN - 0006-291X
VL - 153
SP - 767
EP - 772
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -