L-leucine and its analogue: Specific inhibitors for S-benzyl-L-cysteine-p-nitroanilide-hydrolyzing enzyme in Escherichia coli B

Kousaku Murata; Yoshitaka Iba; Yoshiharu Inoue; Akira Kimura

doi:10.1016/S0006-291X(88)81161-6

L-leucine and its analogue: Specific inhibitors for S-benzyl-L-cysteine-p-nitroanilide-hydrolyzing enzyme in Escherichia coli B

Kousaku Murata, Yoshitaka Iba, Yoshiharu Inoue, Akira Kimura

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	767-772
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	153
Issue number	2
DOIs	https://doi.org/10.1016/S0006-291X(88)81161-6
Publication status	Published - 16-06-1988
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/S0006-291X(88)81161-6

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abstract = "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.",

author = "Kousaku Murata and Yoshitaka Iba and Yoshiharu Inoue and Akira Kimura",

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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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SN - 0006-291X

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SP - 767

EP - 772

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

L-leucine and its analogue: Specific inhibitors for S-benzyl-L-cysteine-p-nitroanilide-hydrolyzing enzyme in Escherichia coli B

Abstract

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