Detection and Characterization of a Thermophilic Biotin Biosynthetic Enzyme, 7-Keto-8-aminopelargonic Acid Synthase, from Various Thermophiles

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By detailed BLAST searches of the genome database of various thermophiles, five ORFs with similarity to the <I>bioF</I> gene, which encodes 7-keto-8-aminopelargonic acid synthase (BioF) involved in biotin biosynthesis, of <I>Escherichia coli</I> were found: <I>AqbioF</I>, <I>CltbioF</I>, <I>GkbioF</I>, <I>SytbioF</I>, and <I>TsebioF</I>, from <I>Aquifex aeolicus</I> VF5, <I>Clostridium thermocellum</I> ATCC27405, <I>Geobacillus kaustophilus</I> JCM12893, <I>Symbiobacterium thermophilum</I> IAM14863, and <I>Thermosynechococcus elongatus</I> BP-1 respectively. The five purified recombinant <I>bioF</I> gene products, which were overexpressed in <I>E. coli</I>, had the enzyme activity of BioF. The optimum temperature range and thermostability of five BioFs, AqBioF, CltBioF, GkBioF, SytBioF, and TseBioF, were higher than those of <I>E. coli</I> BioF. In particular, AqBioF was found to show the highest thermostability of the α-oxoamine synthase family enzymes reported to date. Substrate specificity experiments revealed that SytBioF was also able to catalyze the reaction of 2-amino-3-ketobutyrate CoA ligase, a member of the α-oxoamine synthase family, and that it used acetyl-CoA and glycine as substrates, like the TTHA1582 protein of <I>Thermus thermophilus</I>. The other purified BioFs, AqBioF and GkBioF, did not show any activity with acyl-CoAs and amino acids other than pimeloyl-CoA and <small>L</small>-alanine as substrates.

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  • Bioscience, biotechnology, and biochemistry

    Bioscience, biotechnology, and biochemistry 76(4), 685-690, 2012-04-23

    公益社団法人 日本農芸化学会

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各種コード

  • NII論文ID(NAID)
    10030751453
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09168451
  • NDL 記事登録ID
    023592892
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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