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Anthranilate degradation by a cold-adapted Pseudomonas sp.

Cited 3 time in scopus
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Title
Anthranilate degradation by a cold-adapted Pseudomonas sp.
Other Titles
적온적응성 Pseudomonas sp.에 의한 anthranilate 분해 기작
Authors
Yoo, Miyoun
Kim, Dockyu
Hong, Soon Gyu
Kim, Eungbin
Subject
Microbiology
Keywords
Aromatic; Cold-adaptation; Degradation; Thermolabile enzyme
Issue Date
2015
Citation
Yoo, Miyoun, et al. 2015. "Anthranilate degradation by a cold-adapted Pseudomonas sp.". JOURNAL OF BASIC MICROBIOLOGY, 55(3): 354-362.
Abstract
An alpine soil bacterium Pseudomonas sp. strain PAMC 25931 was characterized as eurypsychrophilic (both psychrophilic and mesotolerant) with a broad temperature range of 5­30°C both for anthranilate (2-aminobenzoate) degradation and concomitant cell growth. Two degradative gene clusters (antABC and catBCA) were detected from a fosmid clone in the PAMC 25931 genomic library;each cluster was confirmed to be specifically induced by anthranilate. When expressed in Escherichia coli, the recombinant AntABC (anthranilate 1,2-dioxygenase, AntDO) converted anthranilate into catechol, exhibiting strict specificity toward anthranilate. Recombinant CatA (catechol 1,2-dioxygenase, C12O) from the organism was active over a broad temperature range (5°C-37°C). However, CatA rapidly lost the enzyme activity when incubated at above 25°C. For example, 1 hour-preincubation at 37°C resulted in 100% loss of enzyme activity, while a counterpart from mesophilic P. putida mt-2 did not show any negative effect on the initial enzyme activity. These results suggest that CatA is a new cold-adapted thermolabile enzyme, which might be a product through the adaptation process of PAMC 25931 to naturally cold environments and contribute to its ability to grow on anthranilate there.
URI
http://repository.kopri.re.kr/handle/201206/6117
DOI
http://dx.doi.org/10.1002/jobm.201300079
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