Literature DB >> 7639513

A thermolabile triosephosphate isomerase from the psychrophile Vibrio sp. strain ANT-300.

E Adler1, J Knowles.   

Abstract

We report the isolation of a gene encoding triosephosphate isomerase (TIM; EC 5.3.1.1) from Vibrio sp. strain ANT-300, a psychrophilic marine eubacterium that grows optimally at 7 degrees C. The deduced primary sequence of this isomerase is 50% identical to Escherichia coli TIM and 37% identical to the isomerase of the psychrotroph Moraxella sp. TA137. Transformation with this gene allowed growth of a TIM-deficient E. coli strain on selective media, but only at temperatures below 30 degrees C. The temperature dependence of this complementation is likely to result from an intrinsic thermolability of the isomerase. Indeed, the TIM activity present in ANT-300 lysates is markedly heat-sensitive, with a half-life of inactivation of 520 s at 25 degrees C.

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Year:  1995        PMID: 7639513     DOI: 10.1006/abbi.1995.1378

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  3 in total

1.  Cloning of triose phosphate isomerase gene from an antarctic psychrophilic Pseudomonas sp. by degenerate and splinkerette PCR.

Authors:  W C See Too; L L Few
Journal:  World J Microbiol Biotechnol       Date:  2010-01-03       Impact factor: 3.312

Review 2.  Application-Oriented Marine Isomerases in Biocatalysis.

Authors:  Antonio Trincone
Journal:  Mar Drugs       Date:  2020-11-21       Impact factor: 5.118

3.  Efficiency of sweet whey fermentation with psychrophilic methanogens.

Authors:  Marcin Dębowski; Ewa Korzeniewska; Joanna Kazimierowicz; Marcin Zieliński
Journal:  Environ Sci Pollut Res Int       Date:  2021-05-02       Impact factor: 4.223

  3 in total

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