Molecular cloning and characterization of an enzyme hydrolyzing p-nitrophenyl α-D-glucoside from Bacillus stearothermophilus SA0301

Atsushi Kobayashi, Takashi Tonozuka, Kimihiko Sato, Mikita Suyama, Jun Sasaki, Batbold Nyamdawaa, Masayoshi Sakaguchi, Yoshiyuki Sakano

研究成果: Article査読

3 被引用数 (Scopus)

抄録

Bacillus stearothermophilus SA0301 produces an extracellular oligo-1,6-glucosidase (bsO16G) that also hydrolyzes p-nitrophenyl α-D-glucoside (Tonozuka et al., J. Appl. Glycosci., 45, 397-400 (1998)). We cloned a gene for an enzyme hydrolyzing p-nitrophenyl α-D-glucoside, which was different from the one mentioned above, from B. stearothermophilus SA0301. The k0/Km values of bsO16G for isomaltotriose and isomaltose were 13.2 and 1.39 s-1·mM-1 respectively, while the newly cloned enzyme did not hydrolyze isomaltotriose, and the k0/Km value for isomaltose was 0.81 s -1·mM-1. The primary structure of the cloned enzyme more closely resembled those of trehalose-6-phosphate hydrolases than those of oligo-1,6-glucosidases, and the cloned enzyme hydrolyzed trehalose 6-phosphate. An open reading frame encoding a protein homologous to the trehalose-specific IIBC component of the phopshotransferase system was also found upstream of the gene for this enzyme.

本文言語English
ページ(範囲)495-499
ページ数5
ジャーナルBioscience, Biotechnology and Biochemistry
70
2
DOI
出版ステータスPublished - 2006

ASJC Scopus subject areas

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学

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