Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Arthrobacter”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 361 records · Page 20Linked to original sources
PubMed2004

Reclassification of Brevibacterium liquefaciens Okabayashi and Masuo 1960 as Arthrobacter nicotianae Giovannozzi-Sermanni 1959.

Brevibacterium liquefaciens ATCC 14929(T) was reclassified as Corynebacterium liquefaciens by Lanéelle et al. (1980). A further study by Stackebrandt et al. (1983) described the same strain, indicating high genomic and chemotaxonomic relatedness to Arthrobacter nicotianae; however, reclassification was not formally proposed. Because of the discrepancies between their previous work and the data of Collins & Kroppenstedt (1983), Lanéelle and colleagues re-examined B. liquefaciens and withdrew their recommendation for the assignment of B. liquefaciens to the genus Corynebacterium (Lanéelle et al., 1984). Formal reclassification of B. liquefaciens as A. nicotianae is now proposed.

Actinomycetales↗
PubMed2004

Reconsideration of Arthrobacter ilicis (Mandel et al. 1961) Collins et al. 1982 as a plant-pathogenic species. Proposal to emend the authority and description of the species. Request for an opinion.

Strains now considered to represent the type strain of Arthrobacter ilicis, described as a pathogen of American holly, are not identical. The designated type strain does not represent this pathogen. However, one of the other strains sourced to the type strain of the pathogen does appear to be authentic, but is not a member of A. ilicis. It is proposed that A. ilicis is an unrelated species, not a pathogen of American holly. The nomenclature of A. ilicis can be rectified by emending the authority and by emending the species description to recognize this species as a novel species that is not a plant pathogen. The pathogen of American holly then becomes a novel pathovar, Curtobacterium flaccumfaciens pv. ilicis. The opinion of the Judicial Commission is sought.

Arthrobacter↗
PubMed2003

A calorimetric characterization of Cr(VI)-reducing Arthrobacter oxydans at different phases of the cell growth cycle.

This is the first of a series of calorimetric studies designed to characterize and understand survival mechanisms of metal-reducing bacteria isolated from metal-polluted environments. In this paper we introduce a new concept of thermal spectrum of the endothermic melting of complex biological systems (e.g., proteins, nucleic acids, ribosomes, membrane structures) in intact cells. All thermal spectra measured are thermograms that describe the temperature dependence of heat capacity change of the complex systems of biologically active substances in bacterial cells. This new concept of thermal spectrum was applied to investigate spectral features from intact cells of Cr(VI)-reducer Arthrobacter oxydans at different points of their growth conditions and stages. Over the temperature range of 40-105 degrees C, we observed that spectral changes are particularly significant in the 40-90 degrees C interval. This may correspond to the orderly changes in subcellular structural elements: proteins, ribosomes and RNA, membranes, and various structural elements of the cell wall during different points of the growth cycle and growth conditions. Spectral changes in the 90-105 degrees C region are less pronounced, implicating that the structural composition of DNA-Protein (DNP) complexes may change little.

Arthrobacter↗
PubMed2003

Crystallization and preliminary X-ray analysis of inorganic polyphosphate/ATP-glucomannokinase from Arthrobacter sp. strain KM.

Inorganic polyphosphate [poly(P)]/ATP-glucomannokinase from Arthrobacter sp. strain KM phosphorylates glucose and mannose, utilizing both ATP and poly(P) as phosphoryl donors. The enzyme was overexpressed in Escherichia coli, purified and crystallized by means of the hanging-drop vapour-diffusion method with ammonium sulfate as the precipitant. The crystals were orthorhombic and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 66.2, b = 83.7, c = 103.8 A. Assuming two molecules per asymmetric unit, V(sol) is 0.49. X-ray diffraction data to 2.83 A have been collected from a single crystal.

Arthrobacter↗
PubMed2003

Expression, crystallization and preliminary X-ray crystallographic studies of Arthrobacter globiformis inulin fructotransferase.

A recombinant form of Arthrobacter globiformis inulin fructotransferase (DFAIII-producing) has been overexpressed in Escherichia coli and purified to homogeneity. Crystals were obtained at 293 K by the hanging-drop vapour-diffusion technique using 0.1 M Na HEPES pH 7.5 buffer containing 1.5 M lithium sulfate as a precipitant. Crystals of the recombinant wild-type enzyme diffracted to better than 1.5 A at 100 K using a synchrotron-radiation source at the Photon Factory. The crystal belonged to space group R32, with unit-cell parameters a = b = 92.02, c = 229.82 A in the hexagonal axes. Assuming the presence of one molecule in the asymmetric unit, the V(M) value for the crystal was 2.15 A(3) Da(-1), indicating a solvent content of 42.8%. Selenomethionine-derivative crystals belonged to a different space group, C2, with unit-cell parameters a = 159.32, b = 91.92, c = 92.58 A, beta = 125.06. Matthews coefficient calculations suggested that the C2 selenomethionine-derivative crystal contained three molecules per asymmetric unit.

Arthrobacter↗
PubMed2004

Crystallization and preliminary X-ray study of isomaltodextranase from Arthrobacter globiformis.

A recombinant isomaltodextranase (1,6-alpha-D-glucan isomaltohydrolase; EC 3.2.1.94) from an Arthrobacter sp. that hydrolyzes dextrans to generate isomaltose was purified and crystallized using the sitting-drop vapour-diffusion method at 293 K. X-ray diffraction data were collected to 1.8 A. The crystals belong to space group C2, with unit-cell parameters a = 199.1, b = 62.7, c = 57.4, beta = 101.4 degrees. Analysis of the Patterson self-rotation function suggests that the crystal contains one protein molecule in the asymmetric unit.

Arthrobacter↗
PubMed2004

Crystallization and preliminary crystallographic analysis of endo-1,3-beta-glucanase from Arthrobacter sp.

Endo-1,3-beta-glucanases hydrolyze internal 1,3-beta-glucosyl linkages. The endo-1,3-beta-glucanase from Arthrobacter sp. was crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to space group P4(1), with unit-cell parameters a = 71.31, c = 60.07 A, and contained one molecule per asymmetric unit. The Matthews coefficient (VM) and the solvent content were 2.35 A3 Da(-1) and 47.63%, respectively. Diffraction data were collected to a resolution of 1.66 A at SPring-8 using a MAR CCD area detector and gave a data set with an overall Rmerge of 5.4% and a completeness of 99.4%.

Arthrobacter↗
PubMed2005

Crystallization and X-ray diffraction analysis of 6-aminohexanoate-dimer hydrolase from Arthrobacter sp. KI72.

To investigate the structure-function relationship between 6-aminohexanoate-dimer hydrolase (EII) from Arthrobacter sp. and a cryptic protein (EII') which shows 88% sequence identity to EII, a hybrid protein (named Hyb-24) of EII and EII' was overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method with ammonium sulfate as a precipitant in MES buffer pH 6.5. The crystal belongs to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 96.37, c = 113.09 A. Diffraction data were collected from native and methylmercuric chloride derivative crystals to resolutions of 1.75 and 1.80 A, respectively.

Amidohydrolases↗
PubMed2006

The copper-containing amine oxidase from Arthrobacter globiformis: refinement at 1.55 and 2.20 A resolution in two crystal forms.

Copper-containing amine oxidases are found in all the major kingdoms of life. They catalyse the oxidation of organic amines in the presence of molecular dioxygen to aldehydes and hydrogen peroxide. The catalytic centres contain a Cu atom and a topaquinone cofactor formed autocatalytically from a tyrosine residue in the presence of Cu and molecular oxygen. The structure of the Cu-containing amine oxidase from Arthrobacter globiformis, which was previously refined at 1.8 A resolution in space group C2 with unit-cell parameters a = 157.84, b = 63.24, c = 91.98 A, beta = 112.0 degrees [Wilce et al. (1997), Biochemistry, 36, 16116-16133], has been re-refined with newly recorded data at 1.55 A resolution. The structure has also been solved and refined at 2.2 A resolution in a new crystal form, space group C2, with unit-cell parameters a = 158.04, b = 64.06, c = 69.69 A, beta = 111.7 degrees.

Amine Oxidase (Copper-Containing)↗
PubMed2006

Crystallization and X-ray diffraction analysis of 6-aminohexanoate-cyclic-dimer hydrolase from Arthrobacter sp. KI72.

6-Aminohexanoate-cyclic-dimer hydrolase (EI) from Arthrobacter sp. KI72 was expressed in Escherichia coli and purified by anion-exchange chromatography. EI was crystallized by the sitting-drop vapour-diffusion method with sodium citrate as precipitant in imidazole buffer pH 8.0. The crystal is hexagonal, with unit-cell parameters a = b = 130.75, c = 58.23 A. Diffraction data were collected from native and mercury(II) dichloride-derivative crystals to resolutions of 1.90 and 2.06 A, respectively.

Amidohydrolases↗
PubMed1996

Uptake and utilization of n-octacosane and n-nonacosane by Arthrobacter nicotianae KCC B35.

Arthrobacter nicotianae KCC B35 isolated from blue-green mats densely covering oil sediments along the Arabian Gulf coast grew well on C10 to C40 n-alkanes as sole sources of carbon and energy. Growth on C20 to C40 alkanes was even better than on C10 to C18 alkanes. Biomass samples incubated for 6 h with n-octacosane (C28) or n-nonacosane (C29) accumulated these compounds as the predominant constituent alkanes of the cell hydrocarbon fractions. The even chain hexadecane C16 and the odd chain pentadecane C15 were the second dominant constituent alkanes in C28 and C29 incubated cells, respectively. n-Hexadecane-incubated cells accumulated in their lipids higher proportions of C16-fatty acids than control cells not incubated with hydrocarbons. On the other hand, C28 and C29-incubated cells did not contain any fatty acids with the equivalent chain lengths, but the fatty acid patterns of the cell lipids suggest that there should have been mid-chain oxidation of these very long chain alkanes. This activity qualifies A. nicotianae KCC B35 to be used in cocktails for bioremediating environments polluted with heavy oil sediments.

Alkanes↗
PubMed1992

Interaction of the regulatory protein NicR1 with the promoter region of the pAO1-encoded 6-hydroxy-D-nicotine oxidase gene of Arthrobacter oxidans.

The D,L-nicotine catabolism of the Gram-positive soil bacterium Arthrobacter oxidans is linked to the presence within the cells of the 160 kb catabolic plasmid pAO1. pAO1-cured cells lost the catabolic enzymes and reintroduction of pAO1 by electroporation into cured cells reestablished the nic+ phenotype. DNA band shift assays with extracts from cured and pAO1+ cells suggested that pAO1 encodes the regulatory protein NicR1. Footprint analysis revealed that two homologous palindromes (IR1 and IR2), present in the 5'-regulatory region of the 6-HDNO gene, were protected from DNase I digestion. Binding of NicR1 to the palindromes is symmetrical, co-operative, and stronger to IR1 containing the 6-HDNO gene promoter than to IR2. Site-directed mutagenesis revealed that steric constraints and sequence requirements for NicR1-binding are located exclusively in the palindromic sequences. Deletions and insertions in the interpalindromic region and in the 6-HDNO promoter -10 sequence had no effect on the binding characteristics of NicR1 to the 6-HDNO regulatory region. Acting as a repressor, NicR1 prevents binding of the E. coli RNA-polymerase to the consensus sigma 70 promoter in vitro. However, the interaction of NicR1 with the 6-HDNO promoter region in extracts of nicotine-induced cells from various growth stages did not differ from that observed with extracts of nicotine-uninduced cells.

Arthrobacter↗
PubMed1994

Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans.

The genes of nicotine dehydrogenase (NDH) were identified, cloned and sequenced from the catabolic plasmid pAO1 of Arthrobacter nicotinovorans. In immediate proximity to this gene cluster is the beginning of the 6-hydroxy-L-niotine oxidase (6-HLNO) gene. NDH is composed of three subunits (A, B and C) of M(r) 30,011, 14,924 and 87,677. It belongs to a family of bacterial hydroxylases with a similar subunit structure; they have molybdopterin dinucleotide, FAD and Fe-S clusters as cofactors. Here the first complete primary structure of a bacterial hydroxylase is provided. Sequence alignments of each of the NDH subunits show similarities to the sequences of eukaryotic xanthine dehydrogenase (XDH) but not to other known molybdenum-containing bacterial enzymes. Based on alignment with XDH it is inferred that the smallest subunit (NDHB) carries an iron-sulphur cluster, that the middle-sized subunit (NDHA) binds FAD, and that the largest NDH subunit (NDHC) corresponds to the molybdopterin-binding domain of XDH. Expression of both the ndh and the 6-hino genes required the presence of nicotine and molybdenum in the culture medium. Tungsten inhibited enzyme activity but not the synthesis of the enzyme protein. The enzyme was found in A. nicotinovorans cells in a soluble form and in a membrane-associated form. In the presence of tungsten the fraction of membrane-associated NDH increased.

Amino Acid Sequence↗
PubMed1976

Specific cleavage and physical mapping of simian-virus-40 DNA by the restriction endonuclease of Arthrobacter luteus.

Simian virus 40 (SV40) DNA (strain 776) is cleaved by the restriction endonuclease from Arthrobacter luteus into 32 specific fragments including 20 large pieces designated Alu-A through T as well as 12 minor products named Alu m1 through m8. These were mapped on the SV40 genome by double digestion experiments. Alu fragments were treated with Hind enzymes and vice versa. Similar reciprocal digestions were also carried out with Hae III enzyme. In this way a detailed cleavage map of the SV40 genome could be constructed.

Arthrobacter↗
PubMed1980

A deficiency of citrate synthase results in constitutive expression of the glyoxylate pathway in Arthrobacter pyridinolis.

Previous studies of Arthrobacter pyridinolis indicated that during the first half of the growth cycle on D-fructose, the organism utilizes a respiration-coupled transport system and exhibits glyoxylate pathway activity; during the second half of the growth cycle, a phosphoenolypyruvate:D-fructose phosphotransferase system is used for transport and no glyoxylate pathway activity is found [Pelliccione et al. (1979) Eur. J. Biochem. 95, 69--75]. A citrate-synthase-deficient mutant had the following properties: (a) high constitutive levels of glyoxylate pathway enzymes on various substrates, while such levels were only found in the wild type when it was grown on acetate; (b) acetyl-CoA levels much higher than in the wild type grown on several different substrates, whereas other metabolite levels were similar in the two strains; and (c) under conditions for induction of the phosphotransferase system, the wild type exhibited at least twice as much phosphotransferase activity as the mutant strain. A mutant lacking acetyl-CoA synthetase exhibited no induction of the glyoxylate pathway in the presence of acetate, although acetate uptake was normal. The results indicate a role for acetyl-CoA as inducer of the glyoxylate pathway. They further suggest a possible role, perhaps indirect, in repression of the phosphotransferase system.

Acetyl Coenzyme A↗
PubMed1986

Methylamine oxidase from Arthrobacter P1. A bacterial copper-quinoprotein amine oxidase.

Methylamine oxidase from Arthrobacter P1 was purified to homogeneity. The enzyme oxidizes primary amines but not tyramine or polyamines like spermine and putrescine. The enzyme activity has a pH optimum of 8.0 with methylamine, and is inhibited by certain cations as well as anions at rather low concentrations. The enzyme has an Mr of 167900, an isoelectric point of 4.6, consists of two (probably identical) subunits (Mr 82250) and contains two copper atoms but no sugar residues. The visible absorption spectra of the enzyme as it is isolated (broad maximum at 480 nm), that of its reduced form obtained on addition of excess of methylamine (maximum at 470 nm) and that of phenylhydrazine-inhibited enzyme (maximum at 440 nm) are very similar to those of eucaryotic copper-containing amine oxidases (EC 1.4.3.6). Also the stoichiometry of inhibition with carbonyl group reagents is similar since the enzyme reacted with only one methylhydrazine. The adduct isolated from copper-free enzyme, treated with 2,4-dinitrophenylhydrazine, was identical to that found in bovine serum amine oxidase treated with this compound after copper removal. This indicates that the enzyme is a copper-quinoprotein amine oxidase, the first example from bacterial origin.

Arthrobacter↗
PubMed1987

6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase.

The nucleotide sequence of the 6-hydroxy-D-nicotine oxidase (6-HDNO) gene of Arthrobacter oxidans is presented. This covalently flavinylated enzyme specifically oxidizes 6-hydroxy-D-nicotine to 6-hydroxy-N-methylmyosmine. Coinduced in the presence of nicotine is a 6-hydroxy-L-nicotine-specific enzyme, 6-hydroxy-L-nicotine oxidase (6-HLNO), with FAD noncovalently bound to the apoprotein. A comparison of the nucleotide-derived amino acid sequence of the 6-HDNO with the amino acid sequence data obtained from the purified 6-HLNO polypeptide suggests that the two enantiozymes expressed within the same cell are genetically unrelated. This conclusion is supported by the finding that the FAD-binding sites of the two enzymes are different. 6-HLNO exhibits at the amino-terminus of the polypeptide chain a dinucleotide-binding site characteristic for many other FAD- and NAD(P)-dependent enzymes. No such sequence was found in the nucleotide-derived amino acid sequence of 6-HDNO.

Amino Acid Sequence↗
PubMed1996

Quinaldine 4-oxidase from Arthrobacter sp. Rü61a, a versatile procaryotic molybdenum-containing hydroxylase active towards N-containing heterocyclic compounds and aromatic aldehydes.

Quinaldine 4-oxidase from Arthrobacter sp. Rü61a, an inducible molybdenum-containing hydroxylase, was purified to homogeneity by an optimized five-step procedure. Molecular oxygen is proposed as physiological electron acceptor. Electrons are also transferred to artificial electron acceptors with E'o > -8 mV. The molybdo-iron/sulfur flavoprotein regiospecifically attacks its N-heterocyclic substrates: isoquinoline and phthalazine are hydroxylated adjacent to the N-heteroatom at Cl, whereas quinaldine, quinoline, cinnoline and quinazoline are hydroxylated at C4. Additionally, the aromatic aldehydes benzaldehyde, salicylaldehyde, vanillin and cinnamaldehyde are oxidized to the corresponding carboxylic acids, whereas short-chain aliphatic aldehydes are not. Quinaldine 4-oxidase is compared to the two molybdenum-containing hydroxylases quinoline 2-oxidoreductase from Pseudomonas putida 86 [Tshisuaka, B., Kappl, R., Hüttermann, J. & Lingens, F. (1993) Biochemistry 32, 12928-12934] and isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7 [Lehmann, M., Tshisuaka, B., Fetzner, S., Röger, P. & Lingens, F. (1994) J. Biol. Chem. 269, 11254-11260] with respect to the substrates converted and the electron-acceptor specificities. These dehydrogenases hydroxylate their N-heterocyclic substrates exclusively adjacent to the heteroatom. Whereas the aldehydes tested are scarcely oxidized by quinoline 2-oxidoreductase, isoquinoline 1-oxidoreductase catalyzes the oxidation of the aromatic aldehydes, although being progressively inhibited. Neither quinoline 2-oxidoreductase nor isoquinoline 1-oxidoreductase transfer electrons to oxygen. Otherwise, the spectrum of electron acceptors used by quinoline 2-oxidoreductase and quinaldine 4-oxidase is identical. However, isoquinoline 1-oxidoreductase differs in its electron-acceptor specificity. Quinaldine 4-oxidase is unusual in its substrate and electron-acceptor specificity. This enzyme is able to function as oxidase or dehydrogenase, it oxidizes aldehydes, and it catalyzes the nucleophilic attack of N-containing heterocyclic compounds at two varying positions depending on the substrate.

Aldehydes↗