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 journalArticlepeer-review

2 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 languageEnglish
Pages (from-to)767-772
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume153
Issue number2
DOIs
Publication statusPublished - 16-06-1988
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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