<i>N</i>-Acetylanthranilate Amidase from<i>Arthrobacter nitroguajacolicus</i>Rü61a, an α/β-Hydrolase-Fold Protein Active towards Aryl-Acylamides and -Esters, and Properties of Its Cysteine-Deficient Variant

Kolkenbrock, Stephan; Parschat, Katja; Beermann, Bernd; Hinz, Hans‐Jürgen; Fetzner, Susanne

doi:10.1128/jb.01085-06

Cited by 15 publications

(10 citation statements)

References 73 publications

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“…The functions of qoxLMS (ORFs 4 to 6) encoding quinal-dine-4-oxidase (Qox), hod (ORF 8) coding for the 2,4-dioxygenase catalyzing heterocyclic ring cleavage, and amq (ORF 9) encoding N-acetylanthranilate amide hydrolase were determined by heterologous gene expression analysis (15,32,41). The physiological role of the 1H-4-oxoquinaldine 3-monooxygenase gene moq (ORF 7) was confirmed by interposon mutagenesis (K. Parschat, unpublished data).…”

Section: Resultsmentioning

confidence: 99%

“…The "upper pathway" of quinaldine degradation, the conversion of quinaldine to anthranilate, is encoded by a gene cluster containing genes encoding quinaldine 4-oxidase (Qox) (41), 1H-4-oxoquinaldine 3-monooxygenase (Moq), a 2,4-dioxygenase (Hod) catalyzing heterocyclic ring cleavage of 1H-3-hydroxy-4-oxoquinaldine to carbon monoxide and N-acetylanthranilate (14,15), and an aryl-acylamidase (Amq) that forms anthranilate and acetate (32) (Fig. 1A).…”

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confidence: 99%

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Complete Nucleotide Sequence of the 113-Kilobase Linear Catabolic Plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61a and Transcriptional Analysis of Genes Involved in Quinaldine Degradation

et al. 2007

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The nucleotide sequence of the linear catabolic plasmid pAL1 from the 2-methylquinoline (quinaldine)-degrading strain Arthrobacter nitroguajacolicus Rü61a comprises 112,992 bp. A total of 103 open reading frames (ORFs) were identified on pAL1, 49 of which had no annotatable function. The ORFs were assigned to the following functional groups: (i) catabolism of quinaldine and anthranilate, (ii) conjugation, and (iii) plasmid maintenance and DNA replication and repair. The genes for conversion of quinaldine to anthranilate are organized in two operons that include ORFs presumed to code for proteins involved in assembly of the quinaldine-4-oxidase holoenzyme, namely, a MobA-like putative molybdopterin cytosine dinucleotide synthase and an XdhC-like protein that could be required for insertion of the molybdenum cofactor. Genes possibly coding for enzymes involved in anthranilate degradation via 2-aminobenzoyl coenzyme A form another operon. These operons were expressed when cells were grown on quinaldine or on aromatic compounds downstream in the catabolic pathway. Single-stranded 3 overhangs of putative replication intermediates of pAL1 were predicted to form elaborate secondary structures due to palindromic and superpalindromic terminal sequences; however, the two telomeres appear to form different structures. Sequence analysis of ORFs 101 to 103 suggested that pAL1 codes for one or two putative terminal proteins, presumed to be covalently bound to the 5 termini, and a multidomain telomere-associated protein (Tap) comprising 1,707 amino acids. Even if the putative proteins encoded by ORFs 101 to 103 share motifs with the Tap and terminal proteins involved in telomere patching of Streptomyces linear replicons, their overall sequences and domain structures differ significantly.Arthrobacter nitroguajacolicus Rü61a, formerly assigned to Arthrobacter ilicis, is able to utilize quinaldine (2-methylquinoline) as a sole source of carbon and energy (27; for a review, see reference 13). The "upper pathway" of quinaldine degradation, the conversion of quinaldine to anthranilate, is encoded by a gene cluster containing genes encoding quinaldine 4-oxidase (Qox) (41), 1H-4-oxoquinaldine 3-monooxygenase (Moq), a 2,4-dioxygenase (Hod) catalyzing heterocyclic ring cleavage of 1H-3-hydroxy-4-oxoquinaldine to carbon monoxide and N-acetylanthranilate (14, 15), and an aryl-acylamidase (Amq) that forms anthranilate and acetate (32) (Fig. 1A). The "lower pathway" (i.e., the mineralization of anthranilate) has been suggested to involve catechol formation and ortho ring cleavage (27) (Fig. 1B). Recently, we found that the ability to convert quinaldine to anthranilate is conferred by the conjugative plasmid pAL1, which was identified as a linear replicon with proteins attached to its 5Ј ends (40).Linear plasmids of gram-positive bacteria were first described in Streptomyces rochei in 1979 (20). Since then, they have been reported to occur in many Streptomyces spp., several rhodococci and mycobacteria, Planobispora rosea, the plant pathogen ...

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

Complete Nucleotide Sequence of the 113-Kilobase Linear Catabolic Plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61a and Transcriptional Analysis of Genes Involved in Quinaldine Degradation

et al. 2007

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“…Arylamidases are widely found in animals, plants, and microorganisms (19). In animals, arylamidases have mainly been studied with respect to neural development (3,24).…”

Section: Discussionmentioning

confidence: 99%

“…have been isolated, and their microbial metabolic pathways have also been elucidated (12,22,25,32,43). To date, the sequence information for the following amide pesticide-hydrolyzing enzymes is available: carbaryl hydrolases CahA and CehA (11,12), phenmedipham hydrolase PCD (26), carbofuran hydrolase Mcd (32), carbendazimhydrolyzing esterase MheI (25), propanil-hydrolyzing amidases Amq, PamH, and PrpH (19,28,42), and phenylurea hydrolases PuhA and LibA (2,34). However, the sequence information and biochemical characterization of amidases that hydrolyze other amide pesticides, such as benzoylurea insecticides, organophosphate insecticides (dimethoate and omethoate), and sulfonylurea herbicides, have not been described.…”

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Cloning of a Novel Arylamidase Gene from Paracoccus sp. Strain FLN-7 That Hydrolyzes Amide Pesticides

Zhang

Yin

Hang

et al. 2012

Appl Environ Microbiol

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bThe bacterial isolate Paracoccus sp. strain FLN-7 hydrolyzes amide pesticides such as diflubenzuron, propanil, chlorpropham, and dimethoate through amide bond cleavage. A gene, ampA, encoding a novel arylamidase that catalyzes the amide bond cleavage in the amide pesticides was cloned from the strain. ampA contains a 1,395-bp open reading frame that encodes a 465-aminoacid protein. AmpA was expressed in Escherichia coli BL21 and homogenously purified using Ni-nitrilotriacetic acid affinity chromatography. AmpA is a homodimer with an isoelectric point of 5.4. AmpA displays maximum enzymatic activity at 40°C and a pH of between 7.5 and 8.0, and it is very stable at pHs ranging from 5.5 to 10.0 and at temperatures up to 50°C. AmpA efficiently hydrolyzes a variety of secondary amine compounds such as propanil, 4-acetaminophenol, propham, chlorpropham, dimethoate, and omethoate. The most suitable substrate is propanil, with K m and k cat values of 29.5 M and 49.2 s ؊1 , respectively. The benzoylurea insecticides (diflubenzuron and hexaflumuron) are also hydrolyzed but at low efficiencies. No cofactor is needed for the hydrolysis activity. AmpA shares low identities with reported arylamidases (less than 23%), forms a distinct lineage from closely related arylamidases in the phylogenetic tree, and has different biochemical characteristics and catalytic kinetics with related arylamidases. The results in the present study suggest that AmpA is a good candidate for the study of the mechanism for amide pesticide hydrolysis, genetic engineering of amide herbicide-resistant crops, and bioremediation of amide pesticide-contaminated environments.A variety of amide compounds are used as pesticides to control insects, pathogens, and weeds in agriculture. These compounds include benzoylurea insecticides (hexaflumuron, diflubenzuron, etc.), organophosphate insecticides with an amide group (dimethoate, omethoate, etc.), carbamate insecticides or herbicides (carbofuran, carbaryl, propham, chlorpropham, etc.), benzimidazole fungicides (carbendazim, benomyl, etc.), acetanilide herbicides (acetochlor, butachlor, propanil, etc.), substituted phenylurea herbicides (diuron, linuron, etc.), and sulfonylurea herbicides (chlorsulfuron, metsulfuron-methyl, etc.) (33). However, the widespread use of amide pesticides has resulted in the contamination of the environment and agricultural products. Moreover, many amide pesticides are hazardous to human health and may damage crops when used improperly (7,8,33). Thus, the removal of amide pesticides from the environment and agricultural products is of paramount importance.Microorganisms play a significant role in the degradation or detoxification of amide pesticides in the environment. Bacterial strains that are able to degrade amide pesticides (carbofuran, carbaryl, acetochlor, carbendazim, dimethoate, etc.) have been isolated, and their microbial metabolic pathways have also been elucidated (12,22,25,32,43). To date, the sequence information for the following amide pesticide-hydrolyzing enzymes is...

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“…Rue61a is initiated by two hydroxylation steps, catalyzed by the molybdenum enzyme quinaldine 4-oxidase (9) and an NADPH-dependent 1H-4-oxoquinaldine 3-monooxygenase. A cofactor-independent dioxygenase subsequently cleaves the intermediate 1H-3-hydroxy-4-oxoquinaldine to carbon monoxide and N-acetylanthranilate (10,11), which is hydrolyzed to acetate and anthranilate by an arylacylamidase (12) (Fig. 1A).…”

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The PaaX-Type Repressor MeqR2 of Arthrobacter sp. Strain Rue61a, Involved in the Regulation of Quinaldine Catabolism, Binds to Its Own Promoter and to Catabolic Promoters and Specifically Responds to Anthraniloyl Coenzyme A

Niewerth¹,

Parschat²,

Rauschenberg³

et al. 2012

Journal of Bacteriology

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The genes coding for quinaldine catabolism in Arthrobacter sp. strain Rue61a are clustered on the linear plasmid pAL1 in two upper pathway operons (meqABC and meqDEF) coding for quinaldine conversion to anthranilate and a lower pathway operon encoding anthranilate degradation via coenzyme A (CoA) thioester intermediates. The meqR2 gene, located immediately downstream of the catabolic genes, codes for a PaaX-type transcriptional repressor. MeqR2, purified as recombinant fusion protein, forms a dimer in solution and shows specific and cooperative binding to promoter DNA in vitro. DNA fragments recognized by MeqR2 contained a highly conserved palindromic motif, 5=-TGACGNNCGTcA-3=, which is located at positions ؊35 to ؊24 of the two promoters that control the upper pathway operons, at positions ؉4 to ؉15 of the promoter of the lower pathway genes and at positions ؉53 to ؉64 of the meqR2 promoter. Disruption of the palindrome abolished MeqR2 binding. The dissociation constants (K D ) of MeqR2-DNA complexes as deduced from electrophoretic mobility shift assays were very similar for the four promoters tested (23 nM to 28 nM). Anthraniloyl-CoA was identified as the specific effector of MeqR2, which impairs MeqR2-DNA complex formation in vitro. A binding stoichiometry of one effector molecule per MeqR2 monomer and a K D of 22 nM were determined for the effector-protein complex by isothermal titration calorimetry (ITC). Quantitative reverse transcriptase PCR analyses suggested that MeqR2 is a potent regulator of the meqDEF operon; however, additional regulatory systems have a major impact on transcriptional control of the catabolic operons and of meqR2.A rthrobacter sp. strain Rue61a, an isolate from sludge of the wastewater treatment plant of a coal tar refinery, is able to utilize quinaldine (2-methylquinoline) as a source of carbon and energy (1, 2). Methylquinolines and related N-heteroaromatic compounds are constituents of coal tar and shale oil. Quinolines are more water soluble than their homocyclic naphthalene analogs, and hence they are more readily transported to subsoil and groundwater if entering the environment, e.g., from abandoned coal processing facilities or from wood-creosoting activities. Many quinoline derivatives are considered toxic and/or mutagenic and thus are of environmental concern. However, quinaldine is used in aquaculture for anesthesia of fish (3). Interestingly, quinaldine is also a possible chemical signal in the urine of the male red fox (4) and the male ferret (5) and a component of the anal sac secretion of skunks (6). Quinoline derivatives of natural origin moreover include a plethora of alkaloids from microbial, animal, and plant sources, especially from the Rutaceae (7). A number of bacterial isolates, mainly aerobes from soil, with the ability to degrade quinoline derivatives have been described in the literature (reviewed in reference 8).Quinaldine degradation by Arthrobacter sp. Rue61a is initiated by two hydroxylation steps, catalyzed by the molybdenum enzyme quinaldine 4-oxidase...

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N-Acetylanthranilate Amidase fromArthrobacter nitroguajacolicusRü61a, an α/β-Hydrolase-Fold Protein Active towards Aryl-Acylamides and -Esters, and Properties of Its Cysteine-Deficient Variant

Cited by 15 publications

References 73 publications

Complete Nucleotide Sequence of the 113-Kilobase Linear Catabolic Plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61a and Transcriptional Analysis of Genes Involved in Quinaldine Degradation

Complete Nucleotide Sequence of the 113-Kilobase Linear Catabolic Plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61a and Transcriptional Analysis of Genes Involved in Quinaldine Degradation

Cloning of a Novel Arylamidase Gene from Paracoccus sp. Strain FLN-7 That Hydrolyzes Amide Pesticides

The PaaX-Type Repressor MeqR2 of Arthrobacter sp. Strain Rue61a, Involved in the Regulation of Quinaldine Catabolism, Binds to Its Own Promoter and to Catabolic Promoters and Specifically Responds to Anthraniloyl Coenzyme A

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