2008年9月
Different substrate specificities of two triazine hydrolases (TrzNs) from Nocardioides species
FEMS MICROBIOLOGY LETTERS
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- 巻
- 286
- 号
- 2
- 開始ページ
- 171
- 終了ページ
- 177
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1111/j.1574-6968.2008.01271.x
- 出版者・発行元
- WILEY-BLACKWELL
Nocardioides sp. strain MTD22 degraded atrazine, ametryn and atraton, as did Arthrobacter aurescens strain TC1 and Nocardioides sp. strain C190. These strains contain trzN, a gene coding for TrzN, triazine hydrolase showing a broad substrate range. However, Nocardioides sp. strain AN3 degraded only atrazine despite containing trzN. These differences in s-triazine degradation are presumed to be due to differences in the amino acid sequences of TrzNs. Consequently, 1371 nucleotides of the trzN coding sequences of strains AN3 and MTD22 were determined. Comparisons of the amino acid sequences of TrzNs indicated that three residues of strain AN3 (Thr(214), His(215) and Gln(241)) were distinct from those of the other three strains (Pro(214), Tyr(215) and Glu(241)). To confirm the relationships between these amino acid sequences and the substrate specificities of TrzNs, wild and chimera trzN genes were constructed and expressed in Escherichia coli cells. Cells expressing wild MTD22 trzN (Pro(214)Tyr(215)Glu(241)) and chimera AN3-MTD22 trzN (Thr(214)His(215)Glu(241)) degraded all s-triazines, but the degradation rate was markedly decreased in AN3-MTD22 trzN. Wild AN3 trzN (Thr(214)His(215)Gln(241)) and chimera MTD22-AN3 trzN (Pro(214)Tyr(215)Gln(241)) degraded only atrazine. These results suggest that the substitution of Glu(241) for Gln(241) significantly decreases enzyme affinity for ametryn and atraton.
Web of Science ® 被引用回数 : 23
Web of Science ® の 関連論文(Related Records®)ビュー
- リンク情報
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- DOI
- https://doi.org/10.1111/j.1574-6968.2008.01271.x
- CiNii Articles
- http://ci.nii.ac.jp/naid/80019778565
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/18671800
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000258402200005&DestApp=WOS_CPL
- ID情報
-
- DOI : 10.1111/j.1574-6968.2008.01271.x
- ISSN : 0378-1097
- CiNii Articles ID : 80019778565
- PubMed ID : 18671800
- Web of Science ID : WOS:000258402200005