論文

査読有り
2002年8月

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

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
  • T Suzuki
  • ,
  • T Nakayama
  • ,
  • T Kurihara
  • ,
  • T Nishino
  • ,
  • N Esaki

66
8
開始ページ
1682
終了ページ
1690
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1271/bbb.66.1682
出版者・発行元
TAYLOR & FRANCIS LTD

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 alpha/beta 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.

リンク情報
DOI
https://doi.org/10.1271/bbb.66.1682
J-GLOBAL
https://jglobal.jst.go.jp/detail?JGLOBAL_ID=200902171104473106
CiNii Articles
http://ci.nii.ac.jp/naid/110002693885
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/12353628
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000177809800010&DestApp=WOS_CPL
ID情報
  • DOI : 10.1271/bbb.66.1682
  • ISSN : 0916-8451
  • eISSN : 1347-6947
  • J-Global ID : 200902171104473106
  • CiNii Articles ID : 110002693885
  • PubMed ID : 12353628
  • Web of Science ID : WOS:000177809800010

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