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PubMed1994

Purification and characterization of a pyrrole-2-carboxylate oxygenase from Arthrobacter strain Py1.

Pyrrole-2-carboxylate oxygenase was purified 8.2-fold to homogeneity from Arthrobacter strain Py1 grown on pyrrole-2-carboxylate as sole carbon, nitrogen, and energy source. FAD and dithioerythritol had to be present during the purification procedure to stabilize the enzyme activity. The molecular mass of the pyrrole-2-carboxylate oxygenase was about 160 kDa by gel filtration chromatography and native gradient PAGE, only one polypeptide of about 60 kDa was present after SDS-PAGE. The FAD content was 2.7 to 3.6 mol FAD per enzyme (160 kDa). The non-covalently bound FAD of the pyrrole-2-carboxylate oxygenase was reduced by NADH and reoxidized by oxygen and pyrrole-2-carboxylate. The enzyme exhibited a narrow substrate specificity. Besides pyrrole-2-carboxylate, only pyrrole, pyrrole-2-aldehyde, and indole-2-carboxylate stimulated the oxygen consumption at a very low rate. The enzyme activity was strongly reduced by different sulfhydryl group inhibitors, but it could be restored by 2-mercaptoethanol or dithiothreitol. The content of pyrrole-2-carboxylate oxygenase was about 6% of the soluble protein as determined by antibodies raised against the enzyme. No cross reacting material was present in other bacteria also able to degrade pyrrole-2-carboxylate. A low amount of the enzyme was present in uninduced cells of Arthrobacter strain Py1, although the enzymatic activity was below the detection limit. The N-terminal amino acid sequence of the enzyme did not contain the consensus sequence GXGXXG found to be present close to the N-terminus of many flavin-dependent monoxygenases sequenced so far.

Amino Acid Sequence↗
PubMedDate not supplied

[Arthrobacter proteinase and its effect on fibrin thrombi].

Arthrobacteria are producers of proteolytic enzymes. Optimal cultivation conditions were determined for Arthrobacter luteus and the mineral composition of the culture medium providing active synthesis of proteinase was optimized. The proteinase was isolated from the culture liquid of Arthrobacter luteus using preparative ion-exchange chromatography on a carboxyl cation exchange resin KMT. The enzyme was homogeneous according to gel chromatography on Sephadex G-200 and had a molecular weight of 24 kD. The fibrinolytic activity of the proteinase is comparable with that of trypsin.

Arthrobacter↗
PubMed2004

A thermostable histamine oxidase from Arthrobacter crystallopoietes KAIT-B-007.

A thermostable histamine oxidase (EC 1.4.3.-) was found in cells of Arthrobacter crystallopoietes KAIT-B-007 isolated from soil. The enzyme was purified about 715-fold over the cell free extracts with a yield of 55% by ammonium sulfate fractionation and various column chromatographies. The purified enzyme was homogeneous on polyacrylamide gel-electrophoresis (native-PAGE). When the enzyme was kept at 65 degrees C and 70 degrees C for 10 min, the activity was fully stable at 65 degrees C and decreased to 9% of the initial level at 70 degrees C. The enzyme was very thermostable. The optimum pH for histamine oxidase activity was found to be at 9.0, and the enzyme was stable over the pH range of 6 to 9. The purified enzyme showed a single protein band on SDS-PAGE and its molecular mass was estimated to be about 81 kDa. The enzyme showed potent activity toward histamine, whereas it was inactive toward putrescine, cadaverine, spermine, and spermidine. Histamine oxidase was inhibited by N,N-diethyldithiocarbamate (DDTC). The inactive enzyme was restored with Cu2+ to 65% of the initial activity, but Cu+ did not enhance the enzyme activity. It is suggested that Cu2+ is essential for expression of histamine oxidase activity. The enzyme was a copper-containing protein having one atom of copper per mol of the enzyme protein as a result of atomic absorption analysis. The N-terminal amino acid sequence of the purified enzyme was different from that of histamine oxidase from Arthrobacter globiformis IFO12137.

Journal Article↗
PubMed1985

Production and Characterization of a Polymer from Arthrobacter sp.

An Arthrobacter sp. isolated from a glucose-sucrose agar plate was found to produce a neutral, extremely viscous, opalescent extracellular polymer. Growth, polymer production, and rheological properties and chemical composition of the isolated polymer were examined. The polymer was found to be substantially different from other arthrobacter polymers. Some unusual properties included irreversible loss of viscosity with high temperature and degradation of the polymer during fermentation and upon storage at 4 degrees C. Other characteristics included dependence on sucrose for polymer production, relative pH stability, increased viscosity with increased salt concentration, and pseudoplasticity. The polymer was found to be composed primarily (if not entirely) of d-fructose. The fructose content and other characteristics suggested that the polymer was a levan.

Journal Article↗
PubMed1986

Identification of eubacteria isolated from leaf cavities of four species of the N-fixing azolla fern as arthrobacter conn and dimmick.

The nutritional and physiological characteristics of 15 isolates from four species of the Azolla fern were determined. Although some minor variation existed in levels of urease activity, ability to utilize xylose, and formation of N(2) gas from NO(3), all 15 isolates were rather similar and believed to represent a single species. These eubacteria exhibited aminopeptidase activity and became viscous when treated with KOH, similar to gram-negative organisms; however, the absence of lipopolysaccharide and 2-keto-3-deoxyoctonate in cell walls indicated that they are truly gram-positive organisms. They are unusual because peptidoglycan could not be detected during most of their growth cycle. The presence of lysine as the major diamino acid in cell wall hydrolysates, the inability to hydrolyze cellulose, and the distinctive developmental pattern with rods and "V" forms present during log phase, becoming progressively shorter until cocci dominated during stationary and death phases, indicated that these organisms belong to the genus Arthrobacter Conn and Dimmick. With the exception of the inability to hydrolyze gelatin, their characteristics are consistent with those of the type species, Arthrobacter globiformis Conn and Dimmick.

Journal Article↗
PubMed1988

Oxidative Pathway from Squalene to Geranylacetone in Arthrobacter sp. Strain Y-11.

The reaction pathway from squalene to trans-geranylacetone in Arthrobacter sp. strain Y-11 was studied. The enzyme or enzymes catalyzing squalene degradation were found to be membrane bound. Stoichiometric analysis of a cell-free system revealed that the ratio of squalene to trans-geranylacetone changed from 1:2 to 1:1 as the reaction proceeded, indicating two steps in geranylacetone formation. The initial step was found to be oxygenase catalyzed, from the absolute requirement for molecular oxygen in geranylacetone formation and the incorporation of O into geranylacetone under O(2) atmosphere. By using [H]squalene as the substrate, we detected an intermediate in the pathway and identified it as 5,9,13-trimethyltetradeca-4,8,12-trienoic acid by mass spectrometry, infrared spectrometry, nuclear magnetic resonance spectrometry, and chemical synthesis. We deduced that squalene was first oxidatively cleaved to geranylacetone and the intermediate, and that the intermediate was further metabolized to geranylacetone. We also synthesized some of the presumptive metabolites, such as 4,8,12-trimethyltrideca-4,8,12-trien-2-one, and confirmed that they served as active precursors for geranylacetone formation. Based on these lines of evidence, we present here the pathway from squalene to trans-geranylacetone in Arthrobacter sp. strain Y-11.

Journal Article↗
PubMed1988

Degradation of the Phosphonate Herbicide Glyphosate by Arthrobacter atrocyaneus ATCC 13752.

Of nine authentic Arthrobacter strains tested, only A. atrocyaneus ATCC 13752 was capable of using the herbicide glyphosate [N-(phosphonomethyl)glycine] as its sole source of phosphorus. Contrary to the previously isolated Arthrobacter sp. strain GLP-1, which degrades glyphosate via sarcosine, A. atrocyaneus metabolized glyphosate to aminomethylphosphonic acid. The carbon of aminomethylphosphonic acid was entirely converted to CO(2). This is the first report on glyphosate degradation by a bacterial strain without previous selection for glyphosate utilization as a source of phosphorus.

Journal Article↗
PubMed1996

Production of two extracellular alkaline phosphatases by a psychrophilic arthrobacter strain.

We surveyed our collection of psychrophilic bacteria to determine the types of phosphatases they produce and whether any had heat-labile activities with potential applications. Assays at different temperatures showed that the activity from one isolate was optimal at 45(deg)C and decreased dramatically above 55(deg)C. This isolate, D10, had the rod-coccus morphological cycle and cell wall amino acids associated with members of the Arthrobacter genus. Interestingly, we found that this strain made two extracellular phosphatases that could be separated by ammonium sulfate fractionation and migration during polyacrylamide gel electrophoresis. One enzyme, designated D10A, hydrolyzed both X-phos (5-bromo-4-chloro-3-indolyl phosphate) and para-nitrophenyl phosphate as substrates and had activity over a broad pH range of 7 to 11. The second enzyme, D10B, lacked activity against X-phos and had a narrow pH range of about 8 to 9. In addition, the D10B enzyme required calcium for activity. The levels of activity of both enzymes decreased for cells grown in media containing more than 100 (mu)M P(infi). These results not only demonstrate the existence of different enzymes from one Arthrobacter strain but also suggest ways in which other studies may have missed phosphatases with unknown requirements.

Journal Article↗
PubMed2001

The formation and structures of cystites of Arthrobacter ureafaciens NRIC 0157T induced by antibiotics.

The cystite formation of Arthrobacter ureafaciens NRIC 0157(T) was induced by some antibiotics, and the addition of tetracycline at a lag phase was effective for cystite formation in YPM liquid medium. Cystites differed from vegetative cells in the cell wall structure, protein content, and water content. Furthermore, the characteristics and structures of cystites induced by tetracycline were similar to those of cystites produced by nutritional imbalance in CT medium. Consequently, various triggers would induce cystite formation. It is interesting that cystite formation was found in part of the Arthrobacter strains and seemed to correlate with the type of peptidoglycan.

Journal Article↗
PubMed2000

Molecular cloning, sequencing, expression, and site-directed mutagenesis of the 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase gene from Arthrobacter spec. Rü61a.

The ring cleaving enzyme 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD)) of Arthrobacter spec. Rü61a is part of the quinaldine degradation pathway. Carbon monoxide and N-acetyl-anthranilate are the products formed by dioxygenolytic cleavage of two C-C bonds in the substrate's pyridine ring. The gene coding for HOD was cloned and sequenced. An isoelectric point of pH 5.40 and a molecular mass of 31,838 Da was deduced from the sequence. HOD is shown to be remarkably similar to 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase (QDO) of Pseudomonas putida 33/1, but not to other dioxygenases described so far. Consensus regions indicative for any chromophoric cofactor or any catalytically relevant metal were not detected. Sequence comparisons and secondary structure predictions revealed HOD as a new member of the alpha/beta hydrolase fold family. Expression in E. coli yielded recombinant catalytically active His-tagged HOD. S101A and D233A, two mutants of HOD, were obtained by site-directed mutagenesis. Since their residual activity is 43.1% and 62.6%, respectively, they probably are of no catalytic relevance although they might play a role in the interaction between enzyme and substrate.

Amino Acid Sequence↗
PubMed2002

Capillary electrophoresis of Cr(VI) reducer Arthrobacter oxydans.

Rapid and effective separation of bacteria Arthrobacter oxydans was performed using capillary electrophoresis. For optimal separation of bacteria the influence of buffer concentration, pH and applied voltage were studied. It was found that the most appropriate conditions for electrophoretic mobility measurements are as follows: applied voltage 6-14 kV; buffer concentration 5-10 mM pH 6-8. At the stationary phase of growth there are always two main heterogeneous peaks. They are connected with the morphology of bacteria as well as with cell aggregation. The heterogeneity of samples may be explained by surface modifications of bacterial cells.

Arthrobacter↗
PubMed2004

Cytosolic NADP phosphatases I and II from Arthrobacter sp. strain KM: implication in regulation of NAD+/NADP+ balance.

NADP phosphatase (NADPase) is an enzyme that converts NADP+ into NAD+ through dephosphorylation of NADP+, and is considered to be one of the possible candidates for regulation of the NAD+/NADP+ balance in vivo. In order to obtain an intrinsic NADPase, the NADP+-degrading activity in a membrane-free cell extract of a Gram-positive bacterium, Arthrobacter sp. strain KM, was first assessed and demonstrated to be mainly achieved through the NADPase reaction, indicating NADPase is essential for degradation of NADP+ and therefore for regulation of the NAD+/NADP+ balance in cytosol. Then, the isolation of cytosolic NADPase was attempted using NADP+ as a substrate. Two NADPase isozymes, designated as NADPases I and II, were purified from the cell extract of the bacterium, and were indicated to be the sole cytosolic NADPases regulating the balance of NAD+/NADP+. NADPases I and II are homodimers of 32 and 30 kDa subunits, respectively, and most active at pH 7-8. The N-terminal amino acid sequences of the two enzymes are similar to each other. Among the biological substrates tested, both enzymes showed the highest activity toward NADP+ and NADPH. AMP, ADP, and pyridoxal 5'-phosphate were also dephosphorylated, but to lower extents. Comparison of the features of NADPases I and II with those of other acid phosphatases possessing NADPase activity suggested that NADPases I and II are novel enzymes participating in regulation of the NAD+/NADP+ balance in the cytosol.

Acid Phosphatase↗
PubMed1988

Degradation of 3-aminophenol by Arthrobacter spec. mA3.

The bacterial strain mA3 capable of utilizing 3-aminophenol as the sole source of carbon, energy and nitrogen for growth was isolated from an enrichment culture and identified as an Arthrobacter species. Utilization of 0.68 mg/ml 3-aminophenol by batch cultures of this organism was characterized by a specific growth rate (mu) of 0.18 h-1 and a yield coefficient (Y) of 0.60. In chemostat cultures of strain mA3 we determined a critical dilution rate (Dc) of 0.175 h-1 by continuous addition of mineral salt medium with 0.5 mg/ml 3-aminophenol. Evidence was obtained that the degradation of catechol by 3-aminophenol induced as well as non-induced cells follows the beta-ketoadipate pathway. The excess ammonium ions, originating from 3-aminophenol degradation and not needed for assimilation were released into the medium. Cells adapted to 3-aminophenol exhibited a high substrate specificity. Among different aromatic substances tested, only catechol and 3,4-dihydroxybenzoate could serve as a carbon source for growth. The importance of the meta position of the amino group for the first step of hydroxylation is discussed in connection with the substrate specificity of whole mA3 cells.

Aminophenols↗
PubMed1992

Metabolic blocks in the degradation of beta-sitosterol by a plasmid-cured strain of Arthrobacter oxydans.

Plasmid-harbouring, sterol-decomposing organism Arthrobacter oxydans 317 was treated with sodium dodecylsulphate to obtain a plasmid-cured strain A. oxydans 317 A1 incapable of utilizing 4-androstene-3,17-dione (AD). The strain 317 A1 was unable to degrade beta-sitosterol side chain completely to form AD but could carry out partial degradation as shown by the accumulation of 3-oxochol-4-en-24-oic acid as a major metabolite and 27-norcholest-4-en-3,24-dione as a minor metabolite. The strain could form 1,4-androstadiene-3,17-dione (ADD) from 3-oxo-23,24-bisnorchol-1,4-dien-22- oic acid (BNC) to a limited extent. The existence of metabolic blocks in the conversion of 3-oxochol-4-en-24-oic acid to 3-oxo-23,24-bis-norchol-4-en-22-oic acid and further conversion to AD by the plasmid-cured strain 317 A1 was suggested. Neither the formation of ADD from AD nor the conversion of AD and ADD to 9 alpha-hydroxy derivatives leading to steroid ring opening could be done by the plasmid-cured strain but the 17 beta-reduction of AD and ADD and 1(2)-reduction of ADD were not affected by the absence of the plasmid. It was proposed that plasmid determines 1(2)-dehydrogenation and 9 alpha-hydroxylation of steroid ring structure in this organism.

Androstadienes↗
PubMed1977

Lysis of intact yeast cells and isolated cell walls by an inducible enzyme system of Arthrobacter GJM-1.

Bacterium Arthrobacter GJM-1 known in the literature as a good producer of alpha-mannanase was found to accumulate in the culture fluid lytic activities against viable yeast cells during growth on isolated cell walls or beta-glucan fractions of yeast. The accumulation of the lytic activities showed an inducible character. The lytic system produced in the medium containing baker's yeast cell walls was capable of complete solubiliaztion of cell wals in vitro. The system lysed viable cells of a number of yeast species and induced their conversion to protoplasts in an osmotically stabilized medium. The lytic system showed different pH and temperature optima when viable cells or isolated cell walls were used as substrates. The pH optimum of the lysis of isolated cell walls was identical with pH optimum of beta-glucanase activities in the crude system. The results pointed out that in the lysis of intact cells, in addition to beta-glucanases, some other factor is involved. Substantial differences in the nature of the outer and the inner surface of cell walls of Saccharomuces cerevisiae were confirmed in this paper based on the different susceptibility to lysis of the cell walls in vivo and in vitro.

Arthrobacter↗
PubMed1982

[Arthrobacter globiformis - a new yeast-lysing bacterium].

A bacterium capable to lyse viable yeast cells was isolated from compost enriched with baker's yeast cells and was identified as Arthrobacter globiformis. The yeast lytic enzyme complex produced by shaking culture was precipitated with ammonium sulfate, dialyzed and lyophilized. The crude residue contained beta-glucanase and alpha-mannanase, yet not chitinase. Optimale carbon sources in the culture medium for a high enzyme synthesis were 0.5% beta-glucan for the production of beta-glucanase, resp., 3% alpha-mannan for the production of alpha-mannanase. Addition of 10% whole died baker's yeast cells to the culture medium effected similar results. The crude enzyme residue released among other things spheroplasts from cells of the yeast Pichia membranaefaciens, Metschnikowia pulcherrima, Hansenula anomala and Candida guilliermondii "H". However, it did not or only weakly lyse viable cells of the yeasts Rhodotorula rubra, Rhodosporidium toruloides and Sporobolomyces roseus. The mutants of Candida guilliermondii "H" with modified glucan, resp., mannan concentrations in the cell walls did not indicate differences in their susceptibility to lysis.

Arthrobacter↗
PubMed1997

Cloning, sequencing, and expression of Arthrobacter protophormiae endo-beta-N-acetylglucosaminidase in Escherichia coli.

The gene encoding endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae (Endo-A) was cloned, and its nucleotide sequence was determined. A single open reading frame consisting of 1935 base pairs and encoding a polypeptide composed of signal peptides of 24 amino acids and a mature protein of 621 amino acids was found. The primary structure of Endo-A exhibited significant homology with FO1F.10 gene product from Caenorhabditis elegans and weak homology with peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase from Flavobacterium meningosepticum and chitinase from Streptomyces olivaceoviridis. However, the enzyme had no significant homology with any previously reported endo-beta-N-acetylglucosaminidases. Transformed Escherichia coli cells carrying the 4.5-kb fragment expressed Endo-A activity. This enzyme activity was detected in the medium as well as in the periplasmic space of cells under the control of the Endo-A gene promoter. The recombinant Endo-A was efficiently isolated from the periplasmic space of the cells. N-terminal sequence analysis revealed that native and recombinant Endo-A have the same N-terminus. Recombinant and native Endo-A also showed very similar optimum pH profiles and transglycosylation activity.

Amino Acid Sequence↗
PubMed1998

Enzymatic synthesis of a neoglycoconjugate by transglycosylation with Arthrobacter endo-beta-N-acetylglucosaminidase: a substrate for colorimetric detection of endo-beta-N-acetylglucosaminidase activity.

The transglycosylation activity of endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae was used for the enzymatic synthesis of a novel oligosaccharide, Man6GlcNAc-p-nitrophenyl-alpha-D-glucose (Man6GlcNAc-Glc-pNP). The reaction was efficiently induced in aqueous solution containing dimethyl sulfoxide. In the medium containing 20% (v/v) dimethyl sulfoxide with 0.1 M Glc-pNP as an acceptor, the transglycosylation attained yields of 75% by high-performance anion-exchange chromatography. The structure of Man6GlcNAc-Glc-pNP was confirmed by ion mass spectrometry and 400 MHz 1H NMR spectrometry. Various endo-beta-N-acetylglucosaminidases hydrolyzed this oligosaccharide and Man6GlcNAc and Glc-pNP were released from the oligosaccharide by endo-beta-N-acetylglucosaminidase digestion. We have established a new procedure for the colorimetric detection of endo-beta-N-acetylglucosaminidase activity using Man6Glc-NAc-Glc-pNP, which is simple as that for other exoglycosidase assays with pNP-glycosides as substrates.

Acetylglucosaminidase↗