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PubMed1983

[Taxonomic position of the genus Mycococcus].

An attempt to elucidate the taxonomic position of the genera Mycococcus has been made. For this purpose the full range of the taxonomically important properties were investigated among microbial cultures preliminary identified as Mycococci. As a result of comparison Mycococcus with Micrococcus the taxonomic status of the genus Mycococcus was no longer confirmed. On the grounds of the published data and the author's experimental results it was concluded that genus Micrococcus was closely related to genus Arthrobacter. The possibility to place the genus Micrococcus within the group of coryneform bacteria is being discussed.

Actinomycetales↗

PubMedDate not supplied

[Growth kinetics of microorganisms with various ecological strategies in a dialysis culture at low specific growth rates].

A dialysis culture was found to be most suitable for studying the metabolism of microorganisms at a low specific growth rate. The biomass of all microorganisms studied in the dialysis culture increased with time in a linear fashion; hence, the energy spent for growth decreased in proportion to a decrease in the specific growth rate. Microorganisms growing in oligotrophous environment (Arthrobacter globiformis and Lipomyces tetrasporus ) spent much less energy comparing to microorganisms from eutrophic habitats (Pseudomonas fluorescens and Debaryomyces formicarius ).

Arthrobacter↗

PubMed1984

[Microbiological studies of ground water polluted with hydrocarbons. 1. Quantitative and qualitative distribution of bacterial populations].

The groundwater, polluted with hydrocarbons, showed large cell numbers during one year of examination: 10(3)-10(4) CFU/ml grown on N-agar after 5 days at 20 degrees C, 10(4)-10(5) CFU/ml grown on water-agar after 8 weeks at 20 degrees C and total cell numbers of 10(5)-10(7)/ml. The bacteria, which were isolated from N-agar, were chiefly Pseudomonas, Flavobacterium, Acinetobacter, and other gramnegative species, Arthrobacter and Bacillus as members of grampositive bacteria. Furthermore the following "physiological' groups were found in the groundwater: ammonium-oxidizing bacteria (MPN 10(1)-10(2)/ml), sulfur-oxidizing bacteria (MPN 10(1)-10(4)/ml), nitrate-reducing bacteria (MPN 10(3)-10(6)/ml), denitrifying bacteria (MPN 10(1)-10(4)/ml), spores of aerobe spore-forming bacteria (2-30/ml), spores of anaerobe spore-forming bacteria (0.2-0.4/ml), manganese-oxidizing bacteria (10(3)-10(4) CFU/ml) and Actinomycetes (0.1-1.0 CFU/ml).

Acinetobacter↗

PubMed1981

Scope and mechanism of carbohydrase action. Stereocomplementary hydrolytic and glucosyl-transferring actions of glucoamylase and glucodextranase with alpha- and beta-D-glucosyl fluoride.

Rhizopus niveus glucoamylase and Arthrobacter globiformis glucodextranase, which catalyze the hydrolysis of starch and dextrans, respectively, to form D-glucose of inverted (beta) configuration, were found to convert both alpha- and beta-D-glucosyl fluoride to beta-D-glucose and hydrogen fluoride. Each enzyme directly hydrolyzes alpha-D-glucosyl fluoride but utilizes th beta-anomer in reactions that require 2 molecules of substrate and yield glucosyl transfer products which are then rapidly hydrolyzed to form beta-D-glucose. Various D-glucopyranosyl compounds serve as acceptors for such reactions. Mixtures of beta-D-glucosyl fluoride and methyl-alpha-D-glucopyranoside[14C], incubated with either enzyme, yielded both methyl-alpha-D-glucopyranosyl-(1 leads to 4)-alpha-D-[14C]glucopyranoside and methyl-alpha-D-glucopyranosyl-(1 leads to 6)-alpha-D-[14C]glucopyranoside. Glucoamylase produced more of the alpha-maltoside; glucodextranase produced more of the alpha-isomaltoside. Thus, both "exo-alpha-glucan hydrolases" emerge as glucosylases that catalyze stereospecifically complementary hydrolytic and transglucosylative reactions with glucosyl donors of opposite configuration. These reactions not only provide a new view of the catalytic capabilities of these supposedly strict hydrolases; they also furnish a basis for defining a detailed mechanism for catalysis. Present results, together with those of several recent studies from this laboratory (especially similar findings obtained with beta-amylase acting on alpha- and beta-maltosyl fluoride (Hehre, E. J., Brewer, C. F., and Genghof, D. S. (1979) J. Biol. Chem. 254, 5942-5950), provide strong new evidence for the functional flexibility of the catalytic groups of carbohydrases.

Arthrobacter↗

PubMedDate not supplied

[Dynamics of populations of microbial antagonists in nonsterile soil].

The interaction between populations was studied with Arthrobacter crystallopoietes and Streptomyces olivocinereus, an actinomycete producing the antibiotic heliomycin active against Gram-positive microorganisms. The two organisms were either cultivated together in a growth medium or the two populations were introduced simultaneously into nonsterile soil at different levels of population density. The antagonism was found in both cases: A. crystallopoietes cells died off when a population of the potential antagonist was added. The density of a population producing the antibiotic had to be sufficiently high for the antagonism to be manifested. The antagonism influenced the dynamics of a population of the antibiotic-sensitive microorganism. The results have confirmed earlier data to the effect that antibiotic synthesis is possible in nonsterile soil.

Anti-Bacterial Agents↗

PubMedDate not supplied

[Bacterial population dynamics in a soil--plant system].

The dynamics of Rhizobium leguminosarum and Arthrobacter crystallopoietes populations introduced into soil at different levels of density was studied in a zone near barley roots. Microbial life with a high rate of growth was found only at the root surface. For A. crystallopoietes, the ultimate bacterial incidence at the root surface was found to depend on the original level of population density. For Rh. leguminosarum, the ultimate incidence was shown to reach an identical level irrespective of the original population density. Apparently, the identical level of stabilization in Rh. leguminosarum and the dependence of the ultimate incidence of A. crystallopoietes on the original population density reflect the peculiarities of ecological strategies displayed by these microorganisms. The introduction of A. crystallopoietes and Rh. leguminosarum into soil had no effect on the dynamics of soil bacteria assayed by the inoculation method.

Arthrobacter↗

PubMedDate not supplied

[3-oxosteroid-delta 1-dehydrogenase localization in Mycobacterium rubrum and Arthobacter globiformis cells].

Osmotically susceptible forms were obtained from Mycobacterium rubrum and Arthrobacter globiformis (Mycobacterium globiforme) cells. The activity of 3-oxosteroid-delta 1-dehydrogenase was comparatively estimated in subcellular fractions after differential centrifugation of cell homogenates prepared either mechanically or by lysis of osmotically susceptible forms. The results indicate that the enzyme is located in the cells of the above microorganisms in both the free state (in the fraction of soluble proteins) and the membrane-bound form.

Arthrobacter↗

PubMedDate not supplied

[Triglycerides of saprophytic mycobacteria].

Triglycerides produced by mycobacteria and arthrobacteria grown in media with hexadecane or glucose were studied by mass spectrometry. In all of the cases, triglycerides were mixtures of homologues. The triglycerides of Arthrobacter ceroformans grown in a medium with hexadecane contained 90% of tripalmitate and 10% of a mixed triglyceride comprising two residues of palmitic acid and one residue of palmitoleinic acid. Mixed triglycerides containing one unsaturated acyl group prevailed in mycobacterial cells grown in a medium with hexadecane. The acyl groups were the residues of C14:0-, C14:1-, C16:0-, C16:1- and C17:1-acids. The position of various acyl residues in mixed triglycerides was established, and the proportions between homologues in a mixture were determined. The triglyceride fraction had a much more complicated composition when themycobacteria were grown in a medium with glucose: the quantity of the major components increased while the amount of the minor components was a complete series of homologues with the molecular weight from 776 to 888.

Alkanes↗

PubMedDate not supplied

[Electrokinetic properties of Arthobacter siderocapsulatus].

The electro-kinetic properties of Arthrobacter siderocapsulatus were determined using microelectrophoresis in alternating electric field. The surface of bacterial cells was shown to bear positive charge within a wide range of pH. The positive charge of the cells should be attributed apparently to the presence of mucous capsules containing manganese dioxide since the growth of the bacterium is known to involve oxidation of manganese or ferrous iron and accumulation of their hydroxides in the capsules. Because of a high respiration rate and the presence of mucous capsules or sheaths, the cells settling on the surface of metals create zones of differential aeration, thus stimulating corrosion. Studies of the electro-kinetic properties of iron bacteria make it possible to develop protective measures against corrosion and are therefore of practical significance.

Aerobiosis↗

PubMed1993

Growth of mycorrhizal fungi in dixenic cultures with bacteria in media of different composition.

Studies were carried out on the effect of bacteria: Arthrobacter globiformis, Bacillus subtilis and Pseudomonas fluorescens on biomass production by three important ectomycorrhizal fungi: Laccaria laccata, Hebeloma crustuliniforme and Rhizopogon vinicolor in media of different composition. It was shown that bacteria stimulated, inhibited or did not affect significantly the biomass production by mycorrhizal fungi. 3-factor ANOVA have shown that although effect of bacteria was statistically significant (p < or = 0.05), composition of medium and its pH affected mycelial growth stronger than bacteria.

Agaricales↗

PubMed1979

Enzymic assay for lecithin in amniotic fluid.

We describe an enzymic method for determining lecithin in amniotic fluid. Phospholipase D from savoy cabbage is used to liberate choline from lecithin, and the liberated choline is oxidized to betaine and hydrogen peroxide by choline oxidase from Arthrobacter globiformis. The hydrogen peroxide forms a colored complex with phenol and 4-aminoantipyrene in the presence of horseradish peroxidase, and this color is measured spectrophotometrically. The method is relatively easy, precise, and accurate, requires less time and sample than other methods, and offers a reliable alternative to the lecithin/sphingomyelin ratio techniques for assessing fetal lung maturity.

Alcohol Oxidoreductases↗

PubMed1975

Covalently bound FAD in d-6-hydroxynicotine oxidase. Immunological studies of D- and L-6-hydroxynicotine oxidase: evidence for a D-enzyme precursor.

Antersera prepared against both enantiozymes, D- and L-6-hydroxynicotine oxidase, formed precipitins in double diffusion tests with their respective antigens only. A mixture of the two antisera caused spur formation of the two precipitin lines obtained with the pure enzymes. Antiserum to L-apoprotein reacted with native L-enzyme and L-apoprotein but not with the D-sspecific enzyme. D-6-hydroxynicotine oxidase activity was inhibited by the anti-D-antiserum, leaving the L-enzyme fully active, while anti-L-antiserum inhibited the L- but not the D-specific activity. The delayed induction of D-6-hydroxynicotine oxidase as compared to the other activities of the nicotine-degrading sequence and the differential immunochemical behavior of the enantiozymes allowed the search for a D-enzyme precursor. In cells harvested 3 hours after the addition of DL-nicotine, the L-enzyme activity was present, whereas no D-enzyme activity could be detected. However, an extract of these cells did form an immunoprecipitin line with anti-D-antiserum. L-6-Hydroxynicotine oxidase, but no D-6-hydroxynicotine oxidase activity, could also be induced in Arthrobacter oxidans grown in a medium with a high glucose content and DL-nicotine as the sole nitrogen source. An extract of these L-induced cells produced the specific immunoprecipitation with anti-D-antiserum. A pulse-chase experiment with cells grown first on glucose and DL-nicotine in the presence of [14C]leucine and then in an unlabeled medium which induces D-6-hydroxynicotine oxidase activity resulted in a radioactive D-enzyme-immunoprecipitin line. From these experiments it is concluded that a precursor of the active D-enzyme is induced simultaneously with the other nicotine-degrading enzymes.

Arthrobacter↗

PubMed1993

[Effect of ozone on airborne microorganisms].

The microbicidal effect of ozone in air was tested at concentrations between 50 and 600 micrograms/m3 against the species: Staphylococcus epidermidis, Micrococcus luteus, Arthrobacter citreus, Bacillus subtilis (veg.), Escherichia coli, Salmonella typhimurium, Serratia marcescens, Pseudomonas fluorescens and Candida albicans. The microorganisms were exposed on membrane filters at 60-75% relative humidity and 21.5-22.5 degrees C. After exposure times between 1 min and 60 min, the filters were incubated on appropriate agar media. The effect of ozone was determined by comparing the number of colonies on exposed filters to the number on nonexposed filters. The die-off curves (colony count against time) proved not to be rectilinear, but to become steeper with increasing time of exposure. Furthermore, the velocity of reduction increased more than proportional with increasing concentration of ozone. Therefore, the bacterial decay seems not to follow first order reaction kinetics. The values presented for k (constant of the velocity of die-off) and D (decimal reduction time) are valid only for narrow ranges of the initial part of the exposure. Concentrations of 50 to 100 micrograms (0)3/m3 for 1 h resulted only in little reduction, whereas 500 to 600 micrograms/m3 for one hour led to 99% reduction in all bacterial species tested. The gram-positive species seemed to be more sensitive than the gram-negative species, C. albicans proved to be more resistant than the bacteria.

Air Microbiology↗

PubMed1996

The species composition of oligotrophic bacterial communities of Lake Balaton--a numerical analysis.

From among the 565 aerobic and facultatively anaerobic, oligotrophic bacterial isolated obtained from the open water region of the Balatonfüred-bay, 58 representative strains were selected for detailed taxonomic-physiological studies and numerical analyses as well as simultaneous comparisons with authentic bacterial strains isolated earlier by Langó (1987) from different water habitat of the Lake Balaton. On the basis of 186 ceded differential diagnostic characteristics involved in these analyses and comparisons, the representative strains were classified into 6 larger similarity groups (I. Micrococcus spp.; II. Arthrobacter "globiformis"; III. Acinetobacter calcoaceticus; IV. Pseudomonas spp. I; V. Pseudomonas spp. II; VI. Aeromonas spp.) which were partly further divided into smaller subgroups of species level (IV.a. Pseudomonas palleronii; V.a. Pseudomonas pseudoalcaligenes; V.b. Pseudomonas acidovorans; V.c. Pseudomonas fluorescens; VI.a. Aeromonas caviae; VI.b. Aeromonas hydrophila).

Acinetobacter↗

PubMed1998

Molecular evolution of hydantoinases.

The complete amino acid sequence of the hydantoinase from Arthrobacter aurescens DSM 3745 has been derived by automated Edman degradation. This is the first ever reported amino acid sequence of a non-ATP-dependent hydantoinase, which hydrolyzes 5'-monosubstituted hydantoin derivatives L-selectively. A homology search performed in protein and nucleic acid databases retrieved only distantly related proteins. All of these are members of the recently described protein superfamily of amidohydrolases related to ureases (Holm and Sander, Proteins 28: 72-82, 1997). Phylogenetic analysis revealed that the novel hydantoinase forms a new branch separate from other hydantoin cleaving enzymes like dihydropyrimidinases (EC 3.5.2.2) and allantoinases (EC 3.5.2.5). Our results suggests that the enzymes of this protein superfamily have evolved from a common ancestor and therefore are the product of divergent evolution. We show further that the enclosed gene families developed very early in evolution, probably prior to the formation of the three domains, Archaea, Eukarya and Bacteria. Hydantoinases related to ATP-dependent N-methylhydantoinases (EC 3.5.2.14) or 5-oxoprolinases (EC 3.5.2.9) do not belong to this superfamily.

Amidohydrolases↗

PubMed1998

Allergic alveolitis among agricultural workers in eastern Poland: a study of twenty cases.

The aim of this study was to identify the specific agents which caused extrinsic allergic alveolitis (EAA) in the selected group of 20 agricultural workers from eastern Poland. The microbiological analysis of the samples of plant materials or dusts reported by the patients as causing symptoms has been carried out, followed by allergological tests (inhalation challenge, agar-gel precipitation test, inhibition of leukocyte migration, skin test) with extrinsic microbial antigens. It was found that the causative agents of allergic alveolitis in the examined group of patients were mesophilic, non-branching bacteria associated with grain dust, mostly Pantoea agglomerans (synonyms: Erwinia herbicola, Enterobacter agglomerans) and Arthrobacter globiformis (each in eight cases). The remaining agents were Alcaligenes faecalis (in two cases), and Brevibacterium linens and Staphylococcus epidermidis (in one case each). On the basis of the clinical picture, the bronchoalveolar lavage (BAL) and allergological tests, the diagnosis of the chronic form of the disease was stated in 14 patients and an acute form - in 6 patients. EAA patients demonstrated in the BAL fluid a typical lymphocytic alveolitis both in terms of percentage and absolute number of lymphocytes. Also, the numbers of eosinophils and neutrophils were significantly higher in EAA patients.

Adult↗

PubMed1996

Cloning of the Penicillium minioluteum gene encoding dextranase and its expression in Pichia pastoris.

The DEX gene encoding an extracellular dextranase was isolated from the genomic DNA library of Penicillium minioluteum by hybridization using the dextranase cDNA as a probe. Comparison of the gene and cDNA sequences revealed that the DEX gene does not contain introns. Amino acid sequences comparison of P. minioluteum dextranase with other reported dextranases reveals a significant homology (29% identity) with a dextranase from Arthrobacter sp. CB-8. The DEX gene fragment encoding a mature protein of 574 amino acids was expressed in the methylotrophic yeast Pichia pastoris by using the SUC2 gene signal sequence from Saccharomyces cerevisiae under control of the alcohol oxidase-1 (AOX1) promoter. Over 3.2 g/l of enzymatically active dextranase was secreted into the medium after induction by methanol. The yeast product was indistinguishable from the native enzyme in specific activity and the N-terminus of both proteins were identical.

Amino Acid Sequence↗

PubMed1997

Role of electrostatics at the catalytic metal binding site in xylose isomerase action: Ca(2+)-inhibition and metal competence in the double mutant D254E/D256E.

The catalytic metal binding site of xylose isomerase from Arthrobacter B3728 was modified by protein engineering to diminish the inhibitory effect of Ca2+ and to study the competence of metals on catalysis. To exclude Ca2+ from Site 2 a double mutant D254E/D256E was designed with reduced space available for binding. In order to elucidate structural consequences of the mutation the binary complex of the mutant with Mg2+ as well as ternary complexes with bivalent metal ions and the open-chain inhibitor xylitol were crystallized for x-ray studies. We determined the crystal structures of the ternary complexes containing Mg2+, Mn2+, and Ca2+ at 2.2 to 2.5 A resolutions, and refined them to R factors of 16.3, 16.6, and 19.1, respectively. We found that all metals are liganded by both engineered glutamates as well as by atoms O1 and O2 of the inhibitor. The similarity of the coordination of Ca2+ to that of the cofactors as well as results with Be2+ weaken the assumption that geometry differences should account for the catalytic noncompetence of this ion. Kinetic results of the D254E/D256E mutant enzyme showed that the significant decrease in Ca2+ inhibition was accompanied by a similar reduction in the enzymatic activity. Qualitative argumentation, based on the protein electrostatic potential, indicates that the proximity of the negative side chains to the substrate significantly reduces the electrostatic stabilization of the transition state. Furthermore, due to the smaller size of the catalytic metal site, no water molecule, coordinating the metal, could be observed in ternary complexes of the double mutant. Consequently, the proton shuttle step in the overall mechanism should differ from that in the wild type. These effects can account for the observed decrease in catalytic efficiency of the D254E/D256E mutant enzyme.

Aldose-Ketose Isomerases↗