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PubMed1982

Metabolism of cyclohexaneacetic acid and cyclohexanebutyric acid by Arthrobacter sp. strain CA1.

A strain of Arthrobacter was isolated by enrichment culture with cyclohexaneacetate as the sole source of carbon and grew with a doubling time of 4.2 h. In addition to growing with cyclohexaneacetate, the organism also grew with cyclohexanebutyrate at concentrations not above 0.05%, and with a variety of alicyclic ketones and alcohols. Oxidation of cyclohexaneacetate proceeded through formation of the coenzyme A (CoA) ester followed by initiation of a beta-oxidation cycle. beta-Oxidation was blocked before the second dehydrogenation step due to the formation of a tertiary alcohol, and the side chain was eliminated as acetyl-CoA by the action of (1-hydroxycyclohexan-1-yl)acetyl-CoA lyase. The cyclohexanone thus formed was degraded by a well-described route that involves ring-oxygen insertion by a biological Baeyer-Villiger oxygenase. All enzymes of the proposed metabolic sequence were demonstrated in cell-free extracts. Arthrobacter sp. strain CA1 synthesized constitutive beta-oxidative enzymes, but further induction of enzymes active toward cyclohexaneacetate and its metabolites could occur during growth with the alicyclic acid. Other enzymes of the sequence, (1-hydroxycyclohexan-1-yl)acetyl-CoA lyase and enzymes of cyclohexanone oxidation, were present at negligible levels in succinate-grown cells but induced by growth with cyclohexaneacetate. The oxidation of cyclohexanebutyrate was integrated into the pathway for cyclohexaneacetate oxidation by a single beta-oxidation cycle. Oxidation of the compound could be divided into two phases. Initial oxidation to (1-hydroxycyclohexan-1-yl)acetate could be catalyzed by constitutive enzymes, whereas the further degradation of (1-hydroxycyclohexan-1-yl)acetate was dependent on induced enzyme synthesis which could be inhibited by chloramphenicol with the consequent accumulation of cyclohexaneacetate and (1-hydroxycyclohexan-1-yl)acetate.

Acetates↗
PubMed1986

Initial reactions of xanthone biodegradation by an Arthrobacter sp.

This study examined the catabolism of xanthone by an Arthrobacter sp. (strain GFB100) capable of growth on xanthone as its main source of carbon and energy. An early catabolic intermediate was 3,4-dihydroxyxanthone. This compound was isolated from the growth medium of a mutant strain of the Arthrobacter sp. which lacked the xanthone-inducible dihydroxyxanthone ring-fission dioxygenase of the wild-type strain. Cell extracts from wild-type xanthone-grown cells oxidized 3,4-dihydroxyxanthone to a yellow ring-fission metabolite. The same yellow compound accumulated in xanthone-grown cultures of a spontaneous mutant which lacked an active, xanthone-inducible, NADPH-linked ring-fission metabolite reductase. The yellow ring-fission metabolite appears to be 4-hydroxy-3-(2'-oxo-3-trans-butenoate)-coumarin, based on its nuclear magnetic resonance spectrum and mass spectral fragmentation pattern, indicating that ring cleavage of 3,4-dihydroxyxanthone was by an extra-diol (meta-fission) mechanism. Enzymatic analyses indicated that growth on xanthone induced a complete gentisate pathway: dioxygenase-catalyzed cleavage of gentisate to maleylpyruvate, isomerization of maleylpyruvate to fumarylpyruvate, and hydrolysis of fumarylpyruvate to fumarate and pyruvate. 4-Hydroxycoumarin was thought to be a likely pathway intermediate linking the early xanthone catabolic steps to the gentisate pathway, since 2-hydroxyacetophenone, a byproduct of 4-hydroxycoumarin hydrolysis, was formed when wild-type cells were cultured with xanthone. Chlorinated 2-hydroxyacetophenones were also obtained from specific chloro-substituted xanthones.

Arthrobacter↗
PubMed1993

Cloning, sequencing, expression, and regulation of the structural gene for the copper/topa quinone-containing methylamine oxidase from Arthrobacter strain P1, a gram-positive facultative methylotroph.

Deoxyoligonucleotides corresponding to amino acid sequences of methylamine oxidase and polyclonal anti-methylamine oxidase antibodies were used to probe Arthrobacter strain P1 plasmid and chromosomal DNA libraries. Two open reading frames, maoxI and maoxII, which are greater than 99% homologous, were cloned from the chromosomal library. The deduced amino acid sequences of the coding regions are identical except for two residues near the C termini. On the other hand, the 5'- and 3'-flanking regions of maoxI and maoxII are quite different. While either gene could code for methylamine oxidase, the dissimilarity in the 5'-flanking regions indicates that the genes are differently regulated. It was determined that maoxII alone encodes methylamine oxidase. The tyrosyl residue which is converted to topa quinone in the mature enzyme was located by comparison with amino acid sequences at the cofactor sites in other copper/topa quinone-containing amine oxidase. Transcriptional start sites and possible regulatory elements were identified in the 5' region of maoxI and maoxII, and stem-loop structures were found in the 3'-flanking regions. High levels of methylamine oxidase are produced when Arthrobacter strain P1 is grown on methylamine alone or on glucose plus methylamine, but growth on LB medium plus methylamine resulted in very low production of the enzyme. Expression of maoxII from its own promoter in Escherichia coli grown on glucose or LB medium with or without methylamine gave the same level of production of methylamine oxidase.

Amino Acid Sequence↗
PubMed1961

Influence of a bacterial cell extract upon the morphogenesis of Arthrobacter ureafaciens.

Blankenship, L. C. (University of Maryland, College Park) and R. N. Doetsch. Influence of a bacterial cell extract upon the morphogenesis of Arthrobacter ureafaciens. J. Bacteriol. 82:882-888. 1961-The effect of a bacterial extract on alleviating the abnormal morphological appearance of Arthrobacter ureafaciens when cultivated in Thiotone broth is described. Physical and chemical analyses of this extract revealed that the mineral components therein were largely responsible for the observed effects. Similar results were obtained using ashed Trypticase soy broth, known mineral mixtures, or magnesium ions. The role played by these materials in governing the morphology of A. ureafaciens is discussed.

Arthrobacter↗
PubMed1962

WHEATON RB: Continuity of psychrophilic and mesophilic growth characteristics in the genus Arthrobacter.

Roth, Norman G. (Whirlpool Corp., St. Joseph, Mich.) and Robert B. Wheaton. Continuity of psychrophilic and mesophilic growth characteristics in the genus Arthrobacter. J. Bacteriol. 83:551-555. 1962.-The effect of temperature on growth of seven members of the genus Arthrobacter was determined at 0, 7, 20, 30, and 37 C. In general, no sharp cutoff point was observed between growth-temperature requirements of psychrophilic and mesophilic bacteria. There appeared to be a continuous gradation among members of this genus in ability to initiate and maintain growth at 0 C. The total number of generations produced was not greatly affected by incubation temperature, provided that growth occurred. However, the time required to attain maximal growth was greatest at psychrophilic temperatures.

Arthrobacter↗
PubMed1973

Isolation and characterization of a bacteriophage of Arthrobacter globiformis.

A bacteriophage which reproduces on Arthrobacter globiformis ATCC 8010 was isolated from soil. This bacteriophage, designated phiAG8010, propagates either in soft agar or broth cultures of the host. Because of a slow adsorption rate, neither the latent period nor burst size was determined. The mature virion belongs to Bradley's group B and exhibits a hexagonal head measuring 69 nm (length) by 60 nm (width) attached to a sheathless tail 120 nm long. The buoyant density of the mature virion is 1.534 g/cm(3). The mature virion contains double-stranded DNA with a buoyant density of 1.722 g/cm(3) (equivalent to 63.3% G + C). Of 14 strains (representing 13 species) of Arthrobacter examined, including A. globiformis ATCC 4336, only A. globiformis ATCC 8010 supported replication of phiAG8010.

Arthrobacter↗
PubMed1975

Differentiation of Arthrobacter soil isolates and named strains from other bacteria by reations on dye-containing media.

Twenty-five gram-negative and 62 gram-positive bacterial cultures, of which 37 werearthrobacters, were tested, using a multipoint inoculation device, for responses on varying concentrations of 35 dyes. Both selective (growth vs. no growth) and differential (dye absorption) responses were obtained. It was possible to differentiate the arthrobacters from the other gram-positive bacteria tested as well as to distinguish separately each Arthrobacter-named strain. The results indicated that dyes have a greater potential for use in selective and differential media than has been presently realized; and the possibility of using dye-reactions as features in taxonomic schemes to differentiate rapidly many of the common genera of soil bacteria is discussed.

Arthrobacter↗
PubMed1977

Arthrobacter sialophilus sp. nov.; a neuraminidase-producing coryneform.

A new species of Arthrobacter is described for which the name A. sialophilus is proposed. The organism was obtained by elective culture from soil using Collocalia mucoid, and can readily be induced in replacement minimal media with appropriate substrates, to form the enzyme neuraminidase. It undergoes sphere-rod-sphere morphogenesis, is gram-variable, non-motile, aerobic, catalase-positive, oxidase-negative, fails to release acid or gas from saccharides, has a GC content of 56.0 mol % and can grow at temperatures up to 45 degrees C. The peptidoglycan composition of its spherical form contains neither diaminopimelic acid nor arabinose as components, but does manifest the presence of glycine. Its generation time at 30 degrees C on tryptone-yeast extract medium is 1.6 h. Accessory growth factors do not appear to be required. The organism, though colorless in the dark, provides a bright yellow water-insoluble pigment after exposure to light. The foregoing combination of properties distinguishes this isolate from other well-described Arthrobacter spp.

Arthrobacter↗
PubMed1994

Levoglucosan dehydrogenase involved in the assimilation of levoglucosan in Arthrobacter sp. I-552.

A levoglucosan (1,6-anhydro-beta-D-glucopyranose)-using bacterium, isolated from soil, was identified. It was shown to belong to the genus Arthrobacter and tentatively named Arthrobacter sp. I-552. A novel enzyme catalyzed the dehydrogenation of levoglucosan to form 1,6-anhydro-beta-D-ribo-hexopyranos-3-ulose (3-keto levoglucosan), using NAD+ as an electron acceptor, i.e. NAD+: 1,6-anhydro-beta-D-glucopyranose oxidoreductase (trivial name: levoglucosan dehydrogenase). This enzyme was purified and characterized. A possible reaction scheme for the glucose formation was proposed. This pathway for levoglucosan use is distinct from those in yeast and fungi.

Amino Acid Sequence↗
PubMed1995

Two-dimensional gel electrophoresis of ribosomal proteins as a novel approach to bacterial taxonomy: application to the genus Arthrobacter.

Ribosomal proteins from 22 strains of 15 different species belong to the genus Arthrobacter were analyzed by an improved two-dimensional gel electrophoresis. Electrophoretograms of ribosomal proteins from 15 type strains had species-specific patterns. Similarity coefficients (SAB values) of ribosomal proteins with mol. wt. of greater than about 20,000, among strains of the same species (DNA relatedness values of more than 61%) were greater than 0.85, but the SAB values among strains of different species were less than 0.60. The N-terminal amino acid sequences of the AL2 proteins, which migrated into similar positions in this method, from 5 type strains were shown to be highly homologous. Our results indicated that ribosomal proteins have been conserved within species during evolution and that the members of the genus Arthrobacter are phylogenetically homogeneous. Thus, ribosomal protein profiles by this method are a potential tool for strain identification.

Amino Acid Sequence↗
PubMed1999

Cloning and sequence analysis of the gene for glucodextranase from Arthrobacter globiformis T-3044 and expression in Escherichia coli cells.

The gld gene for glucodextranase from Arthrobacter globiformis T-3044 was cloned by using a combination of gene walking and probe methods and expressed on the recombinant plasmid pGD8, which was constructed with pUC118, in Escherichia coli cells. The enzyme gene consisted of a unique open reading frame of 3,153 bp. The comparison of the DNA sequence data with the N-terminal and 6 internal amino acid sequences of the purified enzyme secreted from A. globiformis T-3044 suggested the enzyme was translated from mRNA as a secretory precursor with a signal peptide of 28 amino acids residues. The deduced amino acids sequence of the mature enzyme contained 1,023 residues, resulting in a polypeptide with a molecular mass of 107,475 daltons. The deduced sequence showed about 38% identity to that of the glucoamylase from Clostridium sp. G0005. The glucodextranase activity of transformant harboring pGD8 was about 40 mU/ml at 30 degrees C for a 16-h culture. Although the GDase that was produced from the transformant was shorter than authentic GDase by 2 amino acid residues at the N-terminal end side, its enzymatic properties were almost same as the authentic one. Two kinds of genes, dex1 and dex2, for endo-dextranases from A. globiformis T-3044 were also cloned into Escherichia coli cells. The N-terminal of the purified endo-dextranase from A. globiformis T-3044 agreed with the deduced amino acid sequence, after the 33rd alanine residue, of only the dex1 gene for edo-dextranase. This result suggests that the endo-dextranase is translated from mRNA as a secretory precursor with a signal peptide of 32 amino acids residues. The deduced sequence of endo-dextranase 1 and endo-dextranase 2 showed about 93% and 65% identity with that of known endo-dextranase from Arthrobacter sp. CB-8, respectively.

Amino Acid Sequence↗
PubMed2001

Isolation of poly(3-hydroxybutyrate) (PHB)-degrading microorganisms and characterization of PHB-depolymerase from Arthrobacter sp. strain W6.

Microbial degraders of poly(3-hydroxybutyrate) (PHB) were isolated from soil. Arthrobacter sp. strain W6 used not only PHB as a carbon source, but also PHAs such as poly(3-hydroxybutyrate-co-[5%]3-hydroxyvalerate), poly(3-hydroxybutyrate-co-[14%]3-hydroxyvalerate), and poly(3-hydroxybutyrate-co-[22%]3-hydroxyvalerate). PHB-depolymerase was purified to homogeneity from the culture broth of Arthrobacter sp. strain W6 by a procedure involving DEAE- and butyl-Toyopearl column chromatographies. The Mr of the enzyme was estimated to be about 47,000 by SDS-polyacrylamide gel electrophoresis. The enzyme was most active at pH 8.5 and 50 degrees C, and was inhibited by phenylmethylsulfonyl fluoride, Hg2+, Ag+, and Pb2+.

Arthrobacter↗
PubMed2001

Trehalose-producing operon treYZ from Arthrobacter ramosus S34.

Arthrobacter ramosus S34, which produces trehalose from maltooligosaccharide, was isolated. A trehalose-producing operon, treYZ, was cloned from the genome. Expression experiments with treY and treZ confirmed that they coded malto-oligosyltrehalose synthase and malto-oligosyltrehalose trehalohydrolase, respectively. The amino acid sequence of TreY from A. ramosus S34 and that from Arthrobacter sp. Q36 did not show high identity, nor did those of TreZ.

Amino Acid Sequence↗
PubMed2004

Cyclic tetrasaccharide-synthesizing enzymes from Arthrobacter globiformis A19.

A bacterial strain Arthrobacter globiformis A19 producing cyclic tetrasaccharide (CTS) was isolated from soil. The enzymes, 6-alpha-glucosyltransferase (6GT) and 3-alpha-isomaltosyltransferase (IMT), involved in the synthesis of CTS were purified to homogeneity. The molecular and enzymatic properties of IMT from A. globiformis were similar to those of enzymes from Bacillus globisporus C11 and N75. Arthrobacter 6GT had a smaller molecular mass of 108 kDa and a higher optimum pH of 8.4 than the enzymes from strains of B. globisporus. The genes for IMT (ctsY) and 6GT (ctsZ) were cloned from the genome of A. globiformis A19. The two genes linked together in tandem and formed a gene cluster, ctsYZ. Both of the gene products showed similarities to alpha-glucosidases belonging to glycoside hydrolase family 31, and conserved two aspartic acids corresponding to the putative catalytic residues of the family enzymes. The enzymatic system for the production of CTS consisting of 6GT and IMT might be widespread among bacteria.

Amino Acid Sequence↗
PubMedDate not supplied

Degradation of (-)-ephedrine by Pseudomonas putida. Detection of (-)-ephedrine: NAD+-oxidoreductase from Arthrobacter globiformis.

A bacterium utilizing the alkaloid (-)-ephedrine as its sole source of carbon was isolated by an enrichment-culture technique from soil supplemented with 4-benzoyl-1,3-oxazolidinon-(2). The bacterium was indentified as Pseudomonas putida by morphological and physiological studies. The following metabolites were isolated from the culture fluid: methylamine, formaldehyde, methylbenzoylcarbinol (2-hydroxy-1-oxo-1 phenylpropane), benzoid acid, pyrocatechol and cis, cis-muconic acid. A pathway for the degradation of (-)-ephedrine by Pseudomonas putida is proposed and compared with the degradative pathway in Arthrobacter globiformis. The enzyme, which is responsible for the first step in the catabolism of (-)-ephedrine could be demonstrated in extracts from Arthrobacter globiformis. This enzyme catalyses the dehydrogenation of (-)-ephedrine yielding phenylacetylcarbinol/methylbenzoylcarbinol and methylamine. It requires NAD+ as cofactor and exhibits optimal activity at pH 11 in 0.1 M glycine/NaOH buffer. The Km value for (-)-ephedrine is 0.02 mM and for NAD+ 0.11 mM, respectively. No remarkable loss of activity is observed following treatment with EDTA. The enzyme has been shown to react with a wide range of ethanolamines. A slight enrichment was obtained by ammonium sulphate precipitation. The name (-)-ephedrine: NAD+-oxidoreductase (deaminating) is proposed.

Arthrobacter↗
PubMedDate not supplied

[Arthrobacter siderocapsulatus isolated from lake water].

Two microbial strains have been isolated from lake water. The strains oxidize ferrous compounds and manganese. By the structure of microcolonies and the character of deposited oxides of these metals, the strains are identical to the genus Siderocapsa. However, according to their growth cycle and some morpho-physiological characteristics, they were included into the genus Arthrobacter (Corynebacteriaceae). Since these microorganisms differ, by their cultural and morpho-physiological properties, from other species of this genus, they were classed as a new species. Arthrobacter siderocapsulatus nov. sp.

Arthrobacter↗
PubMed1992

[Microbiological production of 3-oxo-bisnorchola-1, 4-dien-22-oic acid from cholesterol by an Arthrobacter 82].

Among nineteen strains of Arthrobacter which showed to be able to decompose cholesterol in preliminary experiments, a strain of Arthrobacter 82 was selected for microbiological production of 3-oxo-bisnorchola-1,4-dien-22-oic-acid (BNC) from cholesterol. The yield is over of 50% weight percent concentration of 0.25% in the presence of cobalt sulfate. The main intermediate in such a conversion process is cholestenone. Lower glucose and higher corn steep liquor concentration were favorable for side chain degradation of cholestenone and more BNC could be produced. BNC was crystallized in acidic solution and obtained by centrifugation. The structure and characteristics of BNC has been identified by means of conventional physical, chemical and spectrometric techniques.

Arthrobacter↗
PubMedDate not supplied

[Distribution of pyrimidine blocks in the DNA of Brevibacterium linens, Arthrobacter globiformis, Nocardia corallina and Nocardia rubra].

The nucleotide composition and the frequency of pyrimidine blocks were studied in DNA of the following bacteria: Brevibacterium linens (Weignamm, 1910) Breed, 1953; Arthrobacter globiformis (Conn, 1928) Conn et Dimmick, 1947; Nocardia corallina (Bergey et al., 1923) Waksman et Henrici, 1948; Nocardia rubra (Krassilnikov, 1949) Waksman et Henrici, 1948. These organisms are classed by some microbiologists as mycobacteria (the Mycobacteriaceae family) while other authors regard them as representatives of three families belonging to two orders. About 60 percent of all pyrimidines in DNA of these bacteria are found in the sequences pur-pyr-pur and pur-pyr-pyr-pur, the number of dipyrimidines being higher than the amount of monopyrimidine nucleotides. The content of dipyrimidine nucleotides in DNA of Nocardia corallina and Nocardia rubra is higher (16.8 mole %) than the content of dipyrimidine blocks in DNA of Brevibacterium linens and Arthrobacter globiformis, in which the quantity of dipyrimidines is almost the same (13.9 and 14.4 mole %). A new characteristic, the selected mean value, is suggested to evaluate differences in the distribution of pyrimidines in DNA.

Arthrobacter↗