Primary structure and catalytic properties of a cold-active esterase from a psychrotroph, acinetobacter sp. strain no. 6. isolated from siberian soil

Takeshi Suzuki, Toru Nakayama, Tatsuo Kurihara, Tokuzo Nishino, Nobuyoshi Esaki

研究成果: Article査読

19 被引用数 (Scopus)

抄録

We cloned a gene coding for a cold-active esterase from a genomic library of Acinetobacter sp. strain No. 6, a psychrotroph isolated from Siberian soil. The gene, aest, encoded a protein of 301 amino acid residues, the deduced sequence of which had less than 17% identity to sequences of known esterases and lipases. However, the esterase seemed to belong to the α/β hydrolase superfamily, because it contained a sequence, Gly-Xaa-Ser-Xaa-Gly (with Xaa an arbitrary amino acid residue), found in most serine hydrolases of this superfamily. Sequence comparison earlier suggested a weak phylogenetic relationship of gene product AEST to the EST group of the esterase-lipase family, which has been found only in eukaryotes. The aest gene was expressed in Escherichia coli BL21(DE3) cells under the control of the T7 promoter, and the expression product was purified to homogeneity and characterized. It catalyzed the hydrolysis of esters with short-chain acyl groups and had lower activation energy and lower thermostability than do mesophilic enzymes, as expected from the cold-adapted nature of this enzyme.

本文言語English
ページ(範囲)1682-1690
ページ数9
ジャーナルBioscience, Biotechnology and Biochemistry
66
8
DOI
出版ステータスPublished - 2002 1月 1

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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