Anthranilate degradation by a cold-adapted Pseudomonas sp.

scientific article

Anthranilate degradation by a cold-adapted Pseudomonas sp. is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1002/JOBM.201300079
P698PubMed publication ID23720227

P2093author name stringSoon Gyu Hong
Dockyu Kim
Miyoun Yoo
Eungbin Kim
P2860cites workIdentification of anthranilate and benzoate metabolic operons of Pseudomonas fluorescens and functional characterization of their promoter regionsQ25255602
The aerobic pseudomonads: a taxonomic studyQ29615280
Diversity of cold-active protease-producing bacteria from arctic terrestrial and marine environments revealed by enrichment cultureQ30987687
The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analysesQ33905710
Cultured bacterial diversity and human impact on alpine glacier cryoconiteQ33946747
Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1.Q33995178
Naturally transformable Acinetobacter sp. strain ADP1 belongs to the newly described species Acinetobacter baylyiQ34316009
Differential degradation of bicyclics with aromatic and alicyclic rings by Rhodococcus sp. strain DK17.Q35599122
Hydrocarbon spills on Antarctic soils: effects and managementQ35716879
Characterization and regulation of the genes for a novel anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1Q35924329
Cloning, DNA Sequencing, and Amino Acid Sequencing of Catechol 1,2-Dioxygenases (Pyrocatechase) from Pseudomonas putida mt-2 and Pseudomonas arvilla C-1Q36690875
Biphenyl dioxygenase from an arctic isolate is not cold adapted.Q36746823
Classification of catechol 1,2-dioxygenase family: sequence analysis of a gene for the catechol 1,2-dioxygenase showing high specificity for methylcatechols from Gram+ aniline-assimilating Rhodococcus erythropolis AN-13.Q36846679
Monocyclic aromatic hydrocarbon degradation by Rhodococcus sp. strain DK17.Q39650110
Characterization of hydrocarbon-degrading microbial populations in contaminated and pristine Alpine soilsQ39774820
Transcriptional regulation of the ant operon, encoding two-component anthranilate 1,2-dioxygenase, on the carbazole-degradative plasmid pCAR1 of Pseudomonas resinovorans strain CA10.Q40175807
New classification system for oxygenase components involved in ring-hydroxylating oxygenationsQ42647393
Pseudomonas, the dominant polycyclic aromatic hydrocarbon-degrading bacteria isolated from Antarctic soils and the role of large plasmids in horizontal gene transferQ42680420
Hydrocarbon degradation and enzyme activities of cold-adapted bacteria and yeastsQ43034175
Aromatic hydrocarbon degradation genes from chronically polluted Subantarctic marine sedimentsQ43742802
Multiplicity of aromatic ring hydroxylation dioxygenase genes in a strong PCB degrader, Rhodococcus sp. strain RHA1 demonstrated by denaturing gradient gel electrophoresis.Q43751325
A survey of indigenous microbial hydrocarbon degradation genes in soils from Antarctica and Brazil.Q47300511
Occurrence and diversity of naphthalene dioxygenase genes in soil microbial communities from the Maritime AntarcticQ48070807
Comparative phylogenetic analysis of microbial communities in pristine and hydrocarbon-contaminated Alpine soilsQ48081410
Fundamentals of Cold-Adapted EnzymesQ58491540
P433issue3
P304page(s)354-362
P577publication date2013-05-29
P1433published inJournal of Basic MicrobiologyQ6294827
P1476titleAnthranilate degradation by a cold-adapted Pseudomonas sp.
P478volume55

Reverse relations

cites work (P2860)
Q26782830Bacterial degradation of monocyclic aromatic amines
Q42136154Catechol biosynthesis from glucose in Escherichia coli anthranilate-overproducer strains by heterologous expression of anthranilate 1,2-dioxygenase from Pseudomonas aeruginosa PAO1.
Q47878315Genetic diversity of catechol 1,2-dioxygenase in the fecal microbial metagenome.
Q88847940Toward Biorecycling: Isolation of a Soil Bacterium That Grows on a Polyurethane Oligomer and Monomer

Search more.