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  • 1
    Online Resource
    Online Resource
    Abstracts of papers presented at the 13th Conference of the Weed Science Society of Israel Abstracts of papers presented at the Third Israeli-Italian Phytopathological Symposium : January 24-25, 1994 The Hebrew University of Jerusalem, Faculty of Agriculture Rehovot, Israel June 14-17, 1994 Kefar haMaccabi, Israel
    Springer Science and Business Media LLC ; 1994
    In:  Phytoparasitica Vol. 22, No. 2 ( 1994-6), p. 115-180
    Details
    In: Phytoparasitica, Springer Science and Business Media LLC, Vol. 22, No. 2 ( 1994-6), p. 115-180
    Type of Medium: Online Resource
    ISSN: 0334-2123 , 1876-7184
    URL: Article
    DOI: 10.1007/BF02980316
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 1994
    detail.hit.zdb_id: 1469840-7
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  • 2
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    Online Resource
    Involvement of the phosphate regulon and the psiD locus in carbon-phosphorus lyase activity of Escherichia coli K-12
    American Society for Microbiology ; 1987
    In:  Journal of Bacteriology Vol. 169, No. 4 ( 1987-04), p. 1753-1756
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 169, No. 4 ( 1987-04), p. 1753-1756
    Abstract: Escherichia coli K-12 can readily mutate to use methylphosphonic acid as the sole phosphorus source by a direct carbon-to-phosphorus (C-P) bond cleavage activity that releases methane and Pi. The in vivo C-P lyase activity is both physiologically and genetically regulated as a member of the phosphate regulon. Since psiD::lacZ(Mu d1) mutants cannot metabolize methylphosphonic acid, psiD may be the structural gene(s) for C-P lyase.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/jb.169.4.1753-1756.1987
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1987
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 3
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    Online Resource
    Immunological demonstration of a unique 3,4-dihydroxyphenylacetate 2,3-dioxygenase in soil Arthrobacter strains
    American Society for Microbiology ; 1992
    In:  Applied and Environmental Microbiology Vol. 58, No. 9 ( 1992-09), p. 2820-2826
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 58, No. 9 ( 1992-09), p. 2820-2826
    Abstract: Many bacteria biosynthesize 3,4-dihydroxyphenylacetate 2,3-dioxygenases for growth on aromatic acids, but gram-negative organisms have been most extensively studied. A gram-positive strain containing 2,3-dioxygenase activity was identified as Arthrobacter strain Mn-1. The 2,3-dioxygenase from strain Mn-1 was purified to homogeneity by fast protein liquid chromatography with a Mono Q anion-exchange column. Rabbit polyclonal antidioxygenase antibodies were prepared. Ouchterlony double-diffusion and Western blotting (immunoblotting) protocols were used to probe the distribution of the Mn-1 dioxygenase antigen in soil bacteria. Fourteen 2,3-dioxygenase-containing Bacillus and Pseudomonas strains did not contain immunologically cross-reactive proteins. Six of eight Arthrobacter strains contained 2,3-dioxygenase activity, and all of them produced cross-reactive proteins. The data presented here suggest that a unique type of dioxygenase is geographically widespread but is taxonomically confined to Arthrobacter soil bacteria.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/aem.58.9.2820-2826.1992
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
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  • 4
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    Online Resource
    Cloning, characterization, and expression of a gene region from Pseudomonas sp. strain ADP involved in the dechlorination of atrazine
    American Society for Microbiology ; 1995
    In:  Applied and Environmental Microbiology Vol. 61, No. 9 ( 1995-09), p. 3373-3378
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 61, No. 9 ( 1995-09), p. 3373-3378
    Abstract: We previously identified a Pseudomonas sp. strain, ADP, which rapidly metabolized atrazine in liquid culture, agar plates, and soils (R. T. Mandelbaum, D. L. Allan, L. P. Wackett, Appl. Environ. Microbiol. 61:1451-1457, 1995). In this study, we report the cloning and partial characterization of a gene region from Pseudomonas sp. strain ADP that encodes atrazine degradation activity. A 22-kb EcoRI genomic DNA fragment, designated pMD1, was shown to encode atrazine dechlorination activity in Escherichia coli DH5 alpha. Atrazine degradation was demonstrated by a zone-clearing assay on agar medium containing crystalline atrazine and by chromatographic methods. A gene conferring the atrazine-clearing phenotype was subsequently subcloned as a 1.9-kb AvaI fragment in pACYC184, designated pMD4, and was expressed in E. coli. This result and random Tn5 mutagenesis established that the 1.9-kb AvaI fragment was essential for atrazine dechlorination. High-pressure liquid and thin-layer chromatographic analyses were used to rigorously establish that E. coli containing pMD4 degraded atrazine and accumulated hydroxyatrazine. Hydroxyatrazine was detected only transiently in E. coli containing pMD1. This is consistent with the idea that hydroxyatrazine is the first metabolite in atrazine degradation by Pseudomonas sp. strain ADP. A 0.6-kb ApaI-PstI fragment from pMD4, containing the putative atrazine chlorohydrolase gene, hybridized to DNA from atrazine-degrading bacteria isolated in Switzerland and Louisiana.(ABSTRACT TRUNCATED AT 250 WORDS)
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/aem.61.9.3373-3378.1995
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1995
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
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  • 5
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    Online Resource
    Bacterial carbon-phosphorus lyase: products, rates, and regulation of phosphonic and phosphinic acid metabolism
    American Society for Microbiology ; 1987
    In:  Journal of Bacteriology Vol. 169, No. 2 ( 1987-02), p. 710-717
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 169, No. 2 ( 1987-02), p. 710-717
    Abstract: Carbon-phosphorus bond cleavage activity, found in bacteria that utilize alkyl- and phenylphosphonic acids, has not yet been obtained in a cell-free system. Given this constraint, a systematic examination of in vivo C-P lyase activity has been conducted to develop insight into the C-P cleavage reaction. Six bacterial strains were obtained by enrichment culture, identified, and characterized with respect to their phosphonic acid substrate specificity. One isolate, Agrobacterium radiobacter, was shown to cleave the carbon-phosphorus bond of a wide range of substrates, including fosfomycin, glyphosate, and dialkyl phosphinic acids. Furthermore, this organism processed vinyl-, propenyl-, and propynylphosphonic acids, a previously uninvestigated group, to ethylene, propene, and propyne, respectively. A determination of product stoichiometries revealed that both C-P bonds of dimethylphosphinic acid are cleaved quantitatively to methane and, furthermore, that the extent of C-P bond cleavage correlated linearly with the specific growth rate for a range of substrates. The broad substrate specificity of Agrobacterium C-P lyase and the comprehensive characterization of the in vivo activity make this an attractive system for further biochemical and mechanistic experiments. In addition, the failure to observe the activity in a group of gram-positive bacteria holds open the possibility that a periplasmic component may be required for in vivo expression of C-P lyase activity.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/jb.169.2.710-717.1987
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1987
    detail.hit.zdb_id: 1481988-0
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  • 6
    Online Resource
    Online Resource
    A manganese-dependent dioxygenase from Arthrobacter globiformis CM-2 belongs to the major extradiol dioxygenase family
    American Society for Microbiology ; 1995
    In:  Journal of Bacteriology Vol. 177, No. 5 ( 1995-03), p. 1225-1232
    Details
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 177, No. 5 ( 1995-03), p. 1225-1232
    Abstract: Almost all bacterial ring cleavage dioxygenases contain iron as the catalytic metal center. We report here the first available sequence for a manganese-dependent 3,4-dihydroxyphenylacetate (3,4-DHPA) 2,3-dioxygenase and its further characterization. This manganese-dependent extradiol dioxygenase from Arthrobacter globiformis CM-2, unlike iron-dependent extradiol dioxygenases, is not inactivated by hydrogen peroxide. Also, ferrous ions, which activate iron extradiol dioxygenases, inhibit 3,4-DHPA 2,3-dioxygenase. The gene encoding 3,4-DHPA 2,3-dioxygenase, mndD, was identified from an A. globiformis CM-2 cosmid library. mndD was subcloned as a 2.0-kb SmaI fragment in pUC18, from which manganese-dependent extradiol dioxygenase activity was expressed at high levels in Escherichia coli. The mndD open reading frame was identified by comparison with the known N-terminal amino acid sequence of purified manganese-dependent 3,4-DHPA 2,3-dioxygenase. Fourteen of 18 amino acids conserved in members of the iron-dependent extradiol dioxygenase family are also conserved in the manganese-dependent 3,4-DHPA 2,3-dioxygenase (MndD). Thus, MndD belongs to the extradiol family of dioxygenases and may share a common ancestry with the iron-dependent extradiol dioxygenases. We propose the revised consensus primary sequence (G,T,N,R)X(H,A)XXXXXXX(L,I,V,M,F)YXX(D,E,T,N,A)PX(G,P) X(2,3)E for this family. (Numbers in brackets indicate a gap of two or three residues at this point in the sequence.) The suggested common ancestry is also supported by sequence obtained from genes flanking mndD, which share significant sequence identity with xylJ and xylG from Pseudomonas putida.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    URL: Article
    DOI: 10.1128/jb.177.5.1225-1232.1995
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1995
    detail.hit.zdb_id: 1481988-0
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  • 7
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    Online Resource
    The atzB gene of Pseudomonas sp. strain ADP encodes the second enzyme of a novel atrazine degradation pathway
    American Society for Microbiology ; 1997
    In:  Applied and Environmental Microbiology Vol. 63, No. 3 ( 1997-03), p. 916-923
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 63, No. 3 ( 1997-03), p. 916-923
    Abstract: We previously reported the isolation of a 21.5-kb genomic DNA fragment from Pseudomonas sp. strain ADP, which contains the atzA gene, encoding the first metabolic step for the degradation of the herbicide atrazine (M. de Souza, L. P. Wackett, K. L. Boundy-Mills, R. T. Mandelbaum, and M. J. Sadowsky, Appl. Environ. Microbiol. 61:3373-3378, 1995). In this study, we show that this fragment also contained the second gene of the atrazine metabolic pathway, atzB. AtzB catalyzed the transformation of hydroxyatrazine to N-isopropylammelide. The product was identified by use of high-performance liquid chromatography, mass spectrometery, and nuclear magnetic resonance spectroscopy. Tn5 mutagenesis of pMD1 was used to determine that atzB was located 8 kb downstream of atzA. Hydroxyatrazine degradation activity was localized to a 4.0-kb ClaI fragment, which was subcloned into the vector pACYC184 to produce plasmid pATZB-2. The DNA sequence of this region was determined and found to contain two large overlapping divergent open reading frames, ORF1 and ORF2. ORF1 was identified as the coding region of atzB by demonstrating that (i) only ORF1 was transcribed in Pseudomonas sp. strain ADP, (ii) a Tn5 insertion in ORF2 did not disrupt function, and (iii) codon usage was consistent with ORF1 being translated. AtzB had 25% amino acid identity with TrzA, a protein that catalyzes a hydrolytic deamination of the s-triazine substrate melamine. The atzA and atzB genes catalyze the first two steps of the metabolic pathway in a bacterium that rapidly metabolizes atrazine to carbon dioxide, ammonia, and chloride.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/aem.63.3.916-923.1997
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1997
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
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  • 8
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    Online Resource
    Mineralization of the s-triazine ring of atrazine by stable bacterial mixed cultures
    American Society for Microbiology ; 1993
    In:  Applied and Environmental Microbiology Vol. 59, No. 6 ( 1993-06), p. 1695-1701
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 59, No. 6 ( 1993-06), p. 1695-1701
    Abstract: Enrichment cultures containing atrazine (2-chloro-4-ethylamino-6-isopropylamino-1,3,5-triazine) at a concentration of 100 ppm (0.46 mM) as a sole nitrogen source were obtained from soils exposed to repeated spills of atrazine, alachlor, and metolachlor. Bacterial growth occurred concomitantly with formation of metabolites from atrazine and subsequent biosynthesis of protein. When ring-labeled [14C]atrazine was used, 80% or more of the s-triazine ring carbon atoms were liberated as 14CO2. Hydroxyatrazine may be an intermediate in the atrazine mineralization pathway. More than 200 pure cultures isolated from the enrichment cultures failed to utilize atrazine as a nitrogen source. Mixing pure cultures restored atrazine-mineralizing activity. Repeated transfer of the mixed cultures led to increased rates of atrazine metabolism. The rate of atrazine degradation, even at the elevated concentrations used, far exceeded the rates previously reported in soils, waters, and mixed and pure cultures of bacteria.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/aem.59.6.1695-1701.1993
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1993
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
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  • 9
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    Online Resource
    Isolation and Characterization of a Pseudomonas sp. That Mineralizes the s-Triazine Herbicide Atrazine
    American Society for Microbiology ; 1995
    In:  Applied and Environmental Microbiology Vol. 61, No. 4 ( 1995-04), p. 1451-1457
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 61, No. 4 ( 1995-04), p. 1451-1457
    Abstract: A bacterium that was capable of metabolizing atrazine at very high concentrations ( 〉 1,000 ppm) was isolated from a herbicide spill site. The organism was differentiated by observing clearing zones on indicator agar plates containing 1,000 ppm atrazine. Detailed taxonomic studies identified the organism as a Pseudomonas sp., designated ADP, that was dissimilar to currently known species. Pseudomonas sp. strain ADP metabolized atrazine as its sole nitrogen source. Nongrowing suspended cells also metabolized atrazine rapidly; for example, 9 x 10(sup9) cells per ml degraded 100 ppm of atrazine in 90 min. Atrazine was metabolized to hydroxyatrazine, polar metabolites, and carbon dioxide. When uniformly ring-labeled [(sup14)C]atrazine was used, 80% of the radioactivity was liberated as (sup14)CO(inf2). These data indicated the triazine ring was completely mineralized. The isolation and characterization of Pseudomonas sp. strain ADP may contribute to efforts on atrazine bioremediation, particularly in environments containing very high pesticide levels.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/aem.61.4.1451-1457.1995
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1995
    detail.hit.zdb_id: 223011-2
    detail.hit.zdb_id: 1478346-0
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  • 10
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    Online Resource
    The University of Minnesota Biocatalysis/Biodegradation Database: specialized metabolism for functional genomics
    Oxford University Press (OUP) ; 1999
    In:  Nucleic Acids Research Vol. 27, No. 1 ( 1999-01-01), p. 373-376
    Details
    In: Nucleic Acids Research, Oxford University Press (OUP), Vol. 27, No. 1 ( 1999-01-01), p. 373-376
    Type of Medium: Online Resource
    ISSN: 0305-1048 , 1362-4962
    URL: Article
    DOI: 10.1093/nar/27.1.373
    RVK:
    WA 15000
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 1999
    detail.hit.zdb_id: 1472175-2
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