Leucine Aminopeptidase from Streptomyces hygroscopicus is Controlled by a Low Molecular Weight Inhibitor

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概要

• 論文の詳細を見る

• In culture filtrate of Streptomyces hygroscopicus a producer of polyketide antibiotics, a leucine aminopeptidase and its autogenous inhibitor were detected. The leucine aminopeptidase was purified 4573-fold with yield of 82% by combination of ion exchange and hydrophobic chromatography. The enzyme is monomeric with a molecular mass of 51 kDa determined by gel chromatography and 67 kDa determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimal activity was at pH 8.0 and 40★. The pI of leucine aminopeptidase is 8.2. The enzyme is strongly inhibited by 1,10-phenantroline, amastatin and dithiothreitol. Atomic absorption spectrometry indicated 2 mols of ion zinc per mol of enzyme. The enzyme is stable at up to 70★. Leucine aminopeptidase prefers leucine and methionine as N-terminal amino acids. Activity of leucine aminopeptidase is strongly modulated by an autogenous low-molecular weight inhibitor during fermentation, especially during periods of intensive antibiotic production.

• 社団法人日本生物工学会の論文
• 2002-10-25

著者

• Izrael Lidija

  School Of Medicine Department Of Chemistry Visegradska

• KARADZIC IVANKA

  School of Medicine, Department of Chemistry, Visegradska

• GOJGIC-CVIJOVIC GORDANA

  Insh,'ute of Chemistry, Technology and Metallurgy, Department of Chemistry, Njegoseva

• VUJCIC ZORAN

  Faculty of Chemistry, Studentski trg

• Gojgic-cvijovic Gordana

  Insh 'ute Of Chemistry Technology And Metallurgy Department Of Chemistry Njegoseva

• Karadzic Ivanka

  School Of Medicine Department Of Chemistry Visegradska

• Vujcic Zoran

  Faculty Of Chemistry Studentski Trg

• Gojgic-Cvijovic Gordana

  Insh,'ute of Chemistry, Technology and Metallurgy, Department of Chemistry, Njegoseva

関連論文

• Leucine Aminopeptidase from Streptomyces hygroscopicus is Controlled by a Low Molecular Weight Inhibitor
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