Anthranilate degradation by a cold-adapted Pseudomonas sp.

Dockyu Kim, Miyoun Yoo, Eungbin Kim, Soon Gyu Hong

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


An alpine soil bacterium Pseudomonas sp. strain PAMC 25931 was characterized as eurypsychrophilic (both psychrophilic and mesotolerant) with a broad temperature range of 5-30°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 (5-37°C). However, CatA rapidly lost the enzyme activity when incubated at above 25°C. For example, 1h-preincubation at 37°C resulted in 100% loss of enzyme activity, while a counterpart from mesophilic Pseudomonas 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.

Original languageEnglish
Pages (from-to)354-362
Number of pages9
JournalJournal of Basic Microbiology
Issue number3
Publication statusPublished - 2015 Mar 1

Bibliographical note

Publisher Copyright:
© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

All Science Journal Classification (ASJC) codes

  • Applied Microbiology and Biotechnology


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