L-leucine and its analogue: specific inhibitors for S-benzyl-L-cysteine-p-nitroanilide-hydrolyzing enzyme in Escherichia coli B.
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.
Murata
K
K
Research Institute for Food Science, Kyoto University, Japan.
Iba
Y
Y
Inoue
Y
Y
Kimura
A
A
D000626:Aminopeptidases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification / Q000378:metabolism; D003545:Cysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D004150:Dipeptidases / Q000302:isolation & purification*; D004151:Dipeptides / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D007930:Leucine / Q000031:analogs & derivatives / Q000494:pharmacology*; D008970:Molecular Weight
D004151:Dipeptides; C028505:cysteinylglycine; C004559:S-benzyl-L-cysteine-4'-nitroanilide; D000626:Aminopeptidases; D004150:Dipeptidases; D007930:Leucine; D003545:Cysteine