Isolation and Characterization of a Dichlorvos-Degrading Strain DDV-1 of Ochrobactrum sp.

Zhang, Xiaohua; Zhang, Guoshun; Zhang, Zhonghui; Xu, Jianhong; Li, Shunpeng

doi:10.1016/s1002-0160(06)60027-1

Cited by 53 publications

(20 citation statements)

References 12 publications

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“…3). Many Ochrobactrum strains were studied for the potential capacity to degrade chemical pollutants and for heavy metal detoxification under a wide range of environmental conditions (24)(25)(26). Another Ochrobactrum strain, DN2, could metabolize nicotine; however, the degradation pathway of strain DN2 is still unknown (9).…”

Section: Discussionmentioning

confidence: 99%

Molecular Mechanism of Nicotine Degradation by a Newly Isolated Strain, Ochrobactrum sp. Strain SJY1

Tang

Zhu

et al. 2015

Appl Environ Microbiol

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A newly isolated strain, SJY1, identified as Ochrobactrum sp., utilizes nicotine as a sole source of carbon, nitrogen, and energy. Strain SJY1 could efficiently degrade nicotine via a variant of the pyridine and pyrrolidine pathways (the VPP pathway), which highlights bacterial metabolic diversity in relation to nicotine degradation. A 97-kbp DNA fragment containing six nicotine degradation-related genes was obtained by gap closing from the genome sequence of strain SJY1. Three genes, designated vppB, vppD, and vppE, in the VPP pathway were cloned and heterologously expressed, and the related proteins were characterized. The vppB gene encodes a flavin-containing amine oxidase converting 6-hydroxynicotine to 6-hydroxy-N-methylmyosmine. Although VppB specifically catalyzes the dehydrogenation of 6-hydroxynicotine rather than nicotine, it shares higher amino acid sequence identity with nicotine oxidase (38%) from the pyrrolidine pathway than with its isoenzyme (6-hydroxy-L-nicotine oxidase, 24%) from the pyridine pathway. The vppD gene encodes an NADH-dependent flavin-containing monooxygenase, which catalyzes the hydroxylation of 6-hydroxy-3-succinoylpyridine to 2,5-dihydroxypyridine. VppD shows 62% amino acid sequence identity with the hydroxylase (HspB) from Pseudomonas putida strain S16, whereas the specific activity of VppD is ϳ10-fold higher than that of HspB. VppE is responsible for the transformation of 2,5-dihydroxypyridine. Sequence alignment and phylogenetic analysis suggested that the VPP pathway, which evolved independently from nicotinic acid degradation, might have a closer relationship with the pyrrolidine pathway. The proteins and functional pathway identified here provide a sound basis for future studies aimed at a better understanding of molecular principles of nicotine degradation. N icotine, which easily passes biological membranes, is significantly harmful to humans and is considered a potentially addictive drug (1, 2). Large quantities of tobacco waste with high concentrations of nicotine are generated annually by cigarette and cigar manufacturing (3). Due to its water solubility, nicotine can easily spread in the environment, emerging as a threat to public health (3). As a result, the U.S. Environmental Protection Agency classified nicotine as a "toxic release inventory" chemical in 1994 (4). Microbes play significant roles in removing nicotine from the environment, and in the meantime, they serve as the catalysts for biotransformation. Nicotine could potentially be used for the production of value-added chemicals. 6-Hydroxy-3-succinoylpyridine (HSP), an important precursor for the synthesis of compounds with biological activities, was efficiently produced by an engineered nicotine-degrading strain (5). Therefore, the study of the mechanism of nicotine degradation provides useful information for both bioremediation and biocatalysis.Many microorganisms that use various nicotine degradation pathways have been isolated from the environment, including Arthrobacter (6), Pseudomonas (7, 8), Ochroba...

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Section: Discussionmentioning

confidence: 99%

Molecular Mechanism of Nicotine Degradation by a Newly Isolated Strain, Ochrobactrum sp. Strain SJY1

Tang

Zhu

et al. 2015

Appl Environ Microbiol

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“…To our knowledge, strain pyd-1 is the first SP-degrading strain reported of the genus Ochrobactrum. Members of this genus are saprophytic soil and water bacteria, and many isolates are responsible for the biodegradation of a wide variety of toxic organic pollutants, such as dichlorvos (Zhang et al 2006), triazophos (Dai et al 2005), p-nitrophenol, methyl parathion (Qiu et al 2006), nicotine (Yuan et al 2007), lindane (Pesce and Wunderlin 2004), naphthalene (Zhang and Peng 2008) and aniline (Wei et al 1998 Strain pyd-1 was capable of degrading a wide range of SPs, including permethrin, fenpropathrin, cypermethrin, cyhalothrin, fenvalerate, deltamethrin and bifenthrin. Permethrin was degraded faster than the other SPs tested, indicating that the additional stereocenter introduced by the a-cyano group causes a relative reduction in the hydrolysis rate.…”

Section: Discussionmentioning

confidence: 99%

Biodegradation of synthetic pyrethroids by Ochrobactrum tritici strain pyd-1

Wang

Zhou

et al. 2011

World J Microbiol Biotechnol

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A synthetic pyrethroid (SP)-degrading bacterium, designated pyd-1, was isolated from SPcontaminated soil. Based on its phenotypic and genotypic properties, the strain was identified as Ochrobactrum tritici. Strain pyd-1 was able to degrade a wide range of SPs, and its degradation efficiencies were dependent on the molecular structure of the SP. Interestingly, the strain degraded cisand trans-permethrin (cypermethrin) at nearly the same rate and possessed approximately equal hydrolysis activities toward the two enantiomers of fenpropathrin. These results suggest that different isomers of SPs are degraded with equal efficiency by strain pyd-1. We studied the metabolic pathway of fenpropathrin degradation in strain pyd-1 by metabolite identification and enzymatic analysis. Fenpropathrin is degraded by hydrolysis of the carboxylester linkage to yield 2,2,3,3-tetramethylcyclopropanecarboxylic acid and 3-phenoxybenzaldehyde, which is converted to 3-phenoxybenzoic acid (PBA). PBA is further metabolized to 4-hydroxy-3-phenoxybenzoic acid (4-hydroxy-PBA). 4-Hydroxy-PBA is oxidized to protocatechuate and p-hydroquinone. Protocatechuate is further oxidized through an ortho-cleavage pathway, and p-hydroquinone is degraded via 1,2,4-benzenetriol.

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“…Soil samples were dried at room temperature, then sieved to 5 mm and stored at 4°C. Soil samples were sterilized as described by Zhang et al (2006). Subsamples (50 g) of fresh soil and sterile soil were weighed, and the solution of isoproturon was added to obtain a final concentration of 30 mg kg -1 of soil, and mixed well.…”

Section: Soil Experimentsmentioning

confidence: 99%

Isolation and characterization of three Sphingobium sp. strains capable of degrading isoproturon and cloning of the catechol 1,2-dioxygenase gene from these strains

Sun

Huang

Chen

et al. 2008

World J Microbiol Biotechnol

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Three strains of bacteria (designated as YBL1, YBL2, YBL3 respectively) capable of degrading isoproturon, 3-(4-isopropylphenyl)-1, 1-dimethylurea, were isolated from the soils of two herbicide plants. Based on the comparative analysis of the 16S rRNA gene, and phenotypic and biochemical characterization, these strains were identified as Sphingobium sp. The optimum conditions for isoproturon degradation by these strains were pH 7.0, and temperature 30°C. Mg 2? (1 mM) enhanced the isoproturon degradation rate, while Ni 2? and Cu 2? (1 mmol l -1 ) inhibited isoproturon degradation significantly. These three strains also showed the ability to remove the residues of other phenylurea herbicides such as chlorotoluron, diuron and fluometuron in mineral salt culture medium. The N-demethylation was the first step of degradation of dimethylurea-substituted herbicides. Strain YBL1 was found capable of degrading both dimethylureasubstituted herbicides and methoxymethylphenyl-urea herbicides i.e. linuron (3-(3,4-dichlorophenyl)-1-methoxy-1-methylurea). Using the PCR method, partial sequences of the catechol 1,2-dioxygenase gene were obtained from these strains.

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Isolation and Characterization of a Dichlorvos-Degrading Strain DDV-1 of Ochrobactrum sp.

Cited by 53 publications

References 12 publications

Molecular Mechanism of Nicotine Degradation by a Newly Isolated Strain, Ochrobactrum sp. Strain SJY1

Molecular Mechanism of Nicotine Degradation by a Newly Isolated Strain, Ochrobactrum sp. Strain SJY1

Biodegradation of synthetic pyrethroids by Ochrobactrum tritici strain pyd-1

Isolation and characterization of three Sphingobium sp. strains capable of degrading isoproturon and cloning of the catechol 1,2-dioxygenase gene from these strains

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