Abstract
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 language | English |
|---|---|
| Pages (from-to) | 354-362 |
| Number of pages | 9 |
| Journal | Journal of Basic Microbiology |
| Volume | 55 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2015 Jan 1 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Applied Microbiology and Biotechnology
Cite this
}
Anthranilate degradation by a cold-adapted Pseudomonas sp. / Kim, Dockyu; Yoo, Miyoun; KIm, Eungbin; Hong, Soon Gyu.
In: Journal of Basic Microbiology, Vol. 55, No. 3, 01.01.2015, p. 354-362.Research output: Contribution to journal › Article
TY - JOUR
T1 - Anthranilate degradation by a cold-adapted Pseudomonas sp.
AU - Kim, Dockyu
AU - Yoo, Miyoun
AU - KIm, Eungbin
AU - Hong, Soon Gyu
PY - 2015/1/1
Y1 - 2015/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84923763836&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84923763836&partnerID=8YFLogxK
U2 - 10.1002/jobm.201300079
DO - 10.1002/jobm.201300079
M3 - Article
VL - 55
SP - 354
EP - 362
JO - Journal of Basic Microbiology
JF - Journal of Basic Microbiology
SN - 0233-111X
IS - 3
ER -