Maturation of an NH_2-Terminallly Extended Thermostable α-Amylase in Bacillus subtilis : A Possible Mechanism Examined by in Vitro Experiments

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概要

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• An artificially inserted extra peptide (21 amino acid peptide) between the B.subtilis α-amylase signal peptide and the mature thermostable α-amylase was completely cleaved by B.subtilis alkaline protease in vitro. The cleavage to form a mature enzyme was observed between pH 7.5 and 10,but not between pH 6.0 and 6.5,although a similar protease activity toward Azocall was observed between pH 6.0 and 7.5. To analyze the effects of pH on the cleavage, CD spectra at pH 6,8,and 11 of the NH_2-terminally extended thermostable α-amylase were analyzed and the results were compared with those of the mature form of the α-amylase. It is suggesteded that the cleavage of the NH_2-terminally extended peptide is controlled by the secondary and tertiary structure of the precursor enzyme. Similar cleavage of different NH_2-terminally extended peptides by the alkaline protease was also found in other hybrid thermostable α-amylases obtained.

• 社団法人日本農芸化学会の論文
• 1992-06-23

著者

• YAMANE Kunio

  Institute of Biological Sciences, University of Tsukuba

• Yamane Kunio

  Institute Of Biological Sciences University Of Tsukuba

• ITOH Yoshiki

  Institute of Biological Sciences, University of Tsukuba

• OGURO Akihiro

  Institute of Biological Sciences, University of Tsukuba

• NAKAMURA Kouji

  Institute of Biological Sciences, University of Tsukuba

• ISHIZUKA Yasuko

  National Chemical Laboratory for Industry

• Itoh Yoshiki

  Institute Of Biological Sciences University Of Tsukuba

• Oguro Akihiro

  Institute Of Biological Sciences University Of Tsukuba

• Nakamura Kouji

  Institute Of Biological Sciences University Of Tsukuba

• YAMANE Kunio

  Institute of Applied Microbiology, The University of Tokyo

関連論文

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• Mutational Site in Tunicamycin-resistant Mutation tmrB8 of Bacillus subtilis as Revealed at the Nucleotide Sequence Level(Microbiology & Fermentation Industry)
• recE-Dependent Gene Amplification Induced by a Tunicamycin-resistant Mutation (tmrA7) in Bacillus subtilis(Microbiology & Fermentation Industry)
• Maturation of an NH_2-Terminallly Extended Thermostable α-Amylase in Bacillus subtilis : A Possible Mechanism Examined by in Vitro Experiments
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• Genetic and Enzymatic Studies on Thermostable α-Amylase of Bacillus subtilis Carrying the Amylase Gene from a Thermophilic Bacterium
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