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Anthranilate degradation by a cold-adapted Pseudomonas sp.

Cited 6 time in wos
Cited 6 time in scopus

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dc.contributor.authorYoo, Miyoun-
dc.contributor.authorKim, Dockyu-
dc.contributor.authorHong, Soon Gyu-
dc.contributor.authorKim, Eungbin-
dc.date.accessioned2018-03-20T13:41:34Z-
dc.date.available2018-03-20T13:41:34Z-
dc.date.issued2015-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/6117-
dc.description.abstractAn 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.-
dc.languageEnglish-
dc.subjectMicrobiology-
dc.titleAnthranilate degradation by a cold-adapted Pseudomonas sp.-
dc.title.alternative적온적응성 Pseudomonas sp.에 의한 anthranilate 분해 기작-
dc.typeArticle-
dc.identifier.bibliographicCitationYoo, Miyoun, et al. 2015. "Anthranilate degradation by a cold-adapted Pseudomonas sp.". <em>JOURNAL OF BASIC MICROBIOLOGY</em>, 55(3): 354-362.-
dc.citation.titleJOURNAL OF BASIC MICROBIOLOGY-
dc.citation.volume55-
dc.citation.number3-
dc.identifier.doi10.1002/jobm.201300079-
dc.citation.startPage354-
dc.citation.endPage362-
dc.description.articleClassificationSCI-
dc.description.jcrRateJCR 2013:70.58823529411765-
dc.subject.keywordAromatic-
dc.subject.keywordCold-adaptation-
dc.subject.keywordDegradation-
dc.subject.keywordThermolabile enzyme-
dc.identifier.localId2014-0027-
dc.identifier.scopusid2-s2.0-84923763836-
dc.identifier.wosid000350644000011-
Appears in Collections  
2011-2013, Utilization of novel metabolites from polar organisms (11-13) / Yim, Joung Han (PE11060, PE12040, PE13040)
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