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The structure of subtilisin ALP I from alkalophilic Bacillus sp. NKS-21

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Abstract

The gene for an alkaline serine protease from alkalophilic Bacillus sp. NKS-21 (subtilisin ALP I) was cloned, and its nucleotide sequence was determined. The gene (aprQ) contained an open reading frame of 1125 bp, encoding a primary product of 374 amino acids. The mature protease, composed of 272 amino acids, was preceded by a putative signal sequence of 37 amino acids and a pro-sequence of 65 amino acids. The mature protease conserved the catalytic triad, Asp, His, and Ser, as subtilisin BPN′ or other subtilisins, and the subtilisin ALP I might belong to the subtilisin super family. The primary structure of subtilisin ALP I was compared and discussed with those of 13 subtilisins, 5 subtilisins from alkalophilic Bacillus, and 8 from neutrophiles. Low homology was shown between subtilisin ALP I and subtilisins from alkalophiles or subtilisins from neutrophiles. Forty-five amino acid residues of the mature protein of subtilisin ALP I were entirely independent of other subtilisins. According to the homology of ALP I with other subtilisins, subtilisin ALP I might be in the middle point between alkaline subtilisins and neutral ones.

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Authors and Affiliations

  1. Laboratory of Molecular Enzymology, Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, 1-1, Tsuysumidori-Amamiyamchi, Aoba-ku, 981, Sendai, Japan

    Youhei Yamagata, Toshihiro Sato & Eiji Ichishima

  2. Laboratory of Biotechnology, Tosoh Co., Hayakawa, 252, Ayase, Japan

    Satoshi Hanzawa

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  1. Youhei Yamagata
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  2. Toshihiro Sato
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  3. Satoshi Hanzawa
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  4. Eiji Ichishima
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Yamagata, Y., Sato, T., Hanzawa, S. et al. The structure of subtilisin ALP I from alkalophilic Bacillus sp. NKS-21. Current Microbiology 30, 201–209 (1995). https://doi.org/10.1007/BF00293634

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