Purification and properties of a peptidase from Nocardia orientalis specific to D-amino acid peptides.

• SUGIE Makiko

  Fermentation Research Institute

• SUZUKI Hideo

  Fermentation Research Institute

• TOMIZUKA Noboru

  Fermentation Research Institute

抄録

A new intracellular peptidase, which we call "D-peptidase S, " was purified from Nocardia orientalis IFO 12806 (ISP 5040). The purified enzyme was homogeneous on disc gel electrophoresis. The molecular weight and the isoelectric point were estimated to be 52, 000 and 4.9, respectively. The optimum pH for the hydrolysis of D-leucyl-D-leucine was 8.0 to 8.1, and the optimum temperature was 36°C. The purified enzyme usually hydrolyzed the peptide bonds preceding the hydrophobic D-amino acids of dipeptides. Tri- and tetra-peptides extending to the amino terminus of such peptides were also hydrolyzed. Therefore, the enzyme is a carboxylpeptidase-like peptidase specific to D-amino acid peptides. The Km values for D-leucyl-D-leucine and L-leucyl-D-leucine were 0.21 × 10^-3 and 0.44×10^-3 M, respectively. The activity was inhibited by several sulfhydryl reagents and two chelators, 8-hydroxyquinoline and o-phenanthroline.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 50 (6), 1397-1402, 1986

  公益社団法人 日本農芸化学会

キーワード

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

詳細情報

• CRID: 1390282681442275584
• NII論文ID: 110006322916
• NII書誌ID: AA00515312
• DOI: 10.1271/bbb1961.50.1397
• ISSN: 18811280
• ISSN: 00021369
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可