Characterization of Sphingomonas sp. Ant 17, an Aromatic Hydrocarbon-Degrading Bacterium Isolated from Antarctic Soil

2002 ◽  
Vol 43 (1) ◽  
pp. 44-54 ◽  
Author(s):  
C.A. Baraniecki ◽  
J. Aislabie ◽  
J.M. Foght
Keyword(s):  
Aromatic Hydrocarbon ◽  
Antarctic Soil ◽  
Degrading Bacterium

scholarly journals Correction: Proteogenomic Characterization of Monocyclic Aromatic Hydrocarbon Degradation Pathways in the Aniline-degrading Bacterium Burkholderia sp. K24

PLoS ONE ◽  
2016 ◽  
Vol 11 (6) ◽  
pp. e0157201
Author(s):  
Sang-Yeop Lee ◽  
Gun-Hwa Kim ◽  
Sung Ho Yun ◽  
Chi-Won Choi ◽  
Yoon-Sun Yi ◽  
...  
Keyword(s):  
Aromatic Hydrocarbon ◽  
Hydrocarbon Degradation ◽  
Degradation Pathways ◽  
Degrading Bacterium

scholarly journals Proteogenomic Characterization of Monocyclic Aromatic Hydrocarbon Degradation Pathways in the Aniline-Degrading Bacterium Burkholderia sp. K24

PLoS ONE ◽  
2016 ◽  
Vol 11 (4) ◽  
pp. e0154233 ◽  
Author(s):  
Sang-Yeop Lee ◽  
Gun-Hwa Kim ◽  
Sung Ho Yun ◽  
Chi-Won Choi ◽  
Yoon-Sun Yi ◽  
...  
Keyword(s):  
Aromatic Hydrocarbon ◽  
Hydrocarbon Degradation ◽  
Degradation Pathways ◽  
Degrading Bacterium

scholarly journals Cloning, Expression, and Characterization of the katGGene, Encoding Catalase-Peroxidase, from the Polycyclic Aromatic Hydrocarbon-Degrading Bacterium Mycobacterium sp. Strain PYR-1

2000 ◽  
Vol 66 (10) ◽  
pp. 4300-4304 ◽  
Author(s):  
Rong-Fu Wang ◽  
David Wennerstrom ◽  
Wei-Wen Cao ◽  
Ashraf A. Khan ◽  
Carl E. Cerniglia
Keyword(s):  
Polycyclic Aromatic Hydrocarbon ◽  
Aromatic Hydrocarbon ◽  
Genomic Library ◽  
Mycobacterium Fortuitum ◽  
Gene Encoding ◽  
Two Dimensional Gel Electrophoresis ◽  
Degrading Bacterium ◽  
Polycyclic Aromatic ◽  
Catalase Peroxidase

ABSTRACT A 81-kDa protein from Mycobacterium sp. strain PYR-1 was expressed in response to exposure of the strain to the polycyclic aromatic hydrocarbon pyrene and recovered by two-dimensional gel electrophoresis. The N-terminal sequence of the protein indicated that it was similar to catalase-peroxidase. An oligonucleotide probe designed from this sequence was used to screen a genomic library ofMycobacterium sp. strain PYR-1, and a positive clone, containing a part of the gene encoding the 81-kDa protein, was isolated. A gene-walking technique was used to sequence the entire gene, which was identified as katG for catalase-peroxidase. The deduced KatG protein sequence showed significant homology to KatGII of Mycobacterium fortuitum and clustered with catalase-peroxidase proteins from other Mycobacteriumspecies in a phylogenetic tree. The katG gene was expressed in Escherichia coli to produce a protein with catalase-peroxidase activity. Since the induction of this catalase-peroxidase occurred in pyrene-induced cultures and the exposure of these cultures to hydrogen peroxide reduced pyrene metabolism, our data suggest that this enzyme plays a role in polycyclic aromatic hydrocarbon metabolism by strain PYR-1.

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