Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans 1 1Edited by J. Karn

Schenk, Susann; Hoelz, André; Krauβ, Beate; Decker, Karl

doi:10.1006/jmbi.1998.2227

Cited by 54 publications

(46 citation statements)

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“…As in the case of kdhL (see legend to Fig. 2B, I, lanes 1 to 3), a gene known to belong to the nicotine regulon of pAO1 (20), transcripts of the genes carrying ORF367 and ORF116 were detected only in bacteria grown in the presence of nicotine in the growth medium (see legend to Cloning of the ORF367gene and purification of the protein. The DNA of ORF367 was cloned into pH6EX3 (3) as an EcoRI-XhoI endonuclease restriction fragment and expressed in Escherichia coli XL-1 Blue.…”

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confidence: 81%

“…1. The nicotine-hydroxylating enzymes, known as nicotine dehydrogenase (NDH) and ketone dehydrogenase (KDH) (8,20), belong to the family of molybdenum cofactor, Fe-S cluster, and flavin adenine dinucleotide (FAD)-dependent hydroxylases (11). 6-Hydroxynicotine oxidases-one specific for 6HLNO and one specific for 6-hydroxy-D-nicotine, a minor side product of nicotine metabolism-are FAD-containing enzymes (5).…”

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confidence: 99%

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An α/β-Fold C—C Bond Hydrolase Is Involved in a Central Step of Nicotine Catabolism by Arthrobacter nicotinovorans

Sachelaru¹,

Schiltz²,

Igloi

et al. 2005

J Bacteriol

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confidence: 81%

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confidence: 99%

An α/β-Fold C—C Bond Hydrolase Is Involved in a Central Step of Nicotine Catabolism by Arthrobacter nicotinovorans

Sachelaru¹,

Schiltz²,

Igloi

et al. 2005

J Bacteriol

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“…Cells were embedded in low-melting-point agarose, lysed using the method of Schenk et al (1998) and equilibrated in TE buffer (10 mM Tris/ HCl, 1 mM EDTA, pH 8). Subsequent proteinase K treatment of the agarose plugs (if appropriate) was performed as described by Schenk et al (1998); however, the samples were incubated for 5 h at 50 uC instead of overnight. PFGE was carried out in a contour-clamped homogeneous electric field apparatus (CHEF-DR III; Bio-Rad) using broad range agarose (1 %, w/v, gels).…”

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confidence: 99%

“…Cell plugs for PFGE were prepared by modifying the method described by Schenk et al (1998). Cells of Arthrobacter spp.…”

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confidence: 99%

“…The washed bacterial cell pellets were preincubated in PIV buffer (1 M NaCl, 1 mM Tris/HCl, pH 7?6) containing 1 mg lysozyme ml 21 (37 uC, 15 min). Cells were embedded in low-melting-point agarose, lysed using the method of Schenk et al (1998) and equilibrated in TE buffer (10 mM Tris/ HCl, 1 mM EDTA, pH 8). Subsequent proteinase K treatment of the agarose plugs (if appropriate) was performed as described by Schenk et al (1998); however, the samples were incubated for 5 h at 50 uC instead of overnight.…”

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Identification of large linear plasmids in Arthrobacter spp. encoding the degradation of quinaldine to anthranilate

et al. 2005

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Arthrobacter nitroguajacolicus Rü 61a, which utilizes quinaldine as sole source of carbon and energy, was shown to contain a conjugative linear plasmid of approximately 110 kb, named pAL1. It exhibits similarities with other linear plasmids from Actinomycetales in that it has proteins covalently attached to its 59 ends. Southern hybridization with probes for the genes encoding quinaldine 4-oxidase and N-acetylanthranilate amidase indicated that pAL1 contains the gene cluster encoding the degradation of quinaldine to anthranilate. A mutant of strain Rü 61a that had lost pAL1 indeed could not convert quinaldine, but was still able to grow on anthranilate. Conjugative transfer of pAL1 to the plasmid-less mutant of strain Rü 61a and to Arthrobacter nicotinovorans DSM 420 (pAO1) occurred at frequencies of 5?4610 "4 and 2?0610per recipient, respectively, and conferred the ability to utilize quinaldine. Five other quinaldine-degrading Gram-positive strains were isolated from soil samples; 16S rDNA sequence analysis suggested the closest relationship to different Arthrobacter species. Except for strain K2-29, all isolates contained a pAL1-like linear plasmid carrying genes encoding quinaldine conversion. A 478 bp fragment that on pAL1 represents an intergenic region showed 100 % sequence identity in all isolates harbouring a pAL1-like plasmid, suggesting horizontal dissemination of the linear plasmid among the genus Arthrobacter. INTRODUCTIONBacteria of the genus Arthrobacter are considered to be ubiquitous in soil and have been found to be among the predominant members of culturable communities from several terrestrial subsurface environments (Crocker et al., 2000). Among the explanations advanced for their ubiquity or even predominance in soil are their resistance to desiccation and nutrient depletion, and their nutritional versatility. Arthrobacter spp. utilize a wide and varied range of natural as well as xenobiotic compounds and thus may play a significant role in the mineralization of organic matter in the environment (Cacciari & Lippi, 1987).Arthrobacter nitroguajacolicus strain Rü61a (formerly assigned to the species Arthrobacter ilicis) utilizes quinaldine (2-methylquinoline), a constituent of coal tar, as sole source of carbon and energy (Hund et al., 1990). Degradation via the anthranilate pathway ( Fig. 1) is initiated by the oxidation of quinaldine to 1H-4-oxoquinaldine, catalysed by quinaldine 4-oxidase (Qox). 1H-4-oxoquinaldine 3-monooxygenase subsequently generates 1H-3-hydroxy-4-oxoquinaldine, which undergoes 2,4-dioxygenolytic ring cleavage to form carbon monoxide and N-acetylanthranilate. This unusual mode of ring cleavage is catalysed by a cofactor-less 2,4-dioxygenase that does not share any similarity with aromatic ring cleavage dioxygenases, but seems to belong to the a/b-hydrolase fold superfamily of proteins (Fetzner, 2002). In the next step, an amidase (Amq) catalyses the hydrolysis of N-acetylanthranilate to anthranilate. We have characterized the gene cluster encoding this 'upper part' of th...

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(S)-6-Hydroxynicotine oxidase

Springer Handbook of Enzymes

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Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans 1 1Edited by J. Karn

Cited by 54 publications

References 68 publications

An α/β-Fold C—C Bond Hydrolase Is Involved in a Central Step of Nicotine Catabolism by Arthrobacter nicotinovorans

An α/β-Fold C—C Bond Hydrolase Is Involved in a Central Step of Nicotine Catabolism by Arthrobacter nicotinovorans

Identification of large linear plasmids in Arthrobacter spp. encoding the degradation of quinaldine to anthranilate

(S)-6-Hydroxynicotine oxidase

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