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PubMed1993

Cloning, sequence analysis, and expression of the Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli.

The pcpB gene of Flavobacterium sp. strain ATCC 39723 was cloned by using a degenerate primer designed from the N-terminal sequence of the purified enzyme. The nucleotide sequence of pcpB was determined and found to encode an open reading frame of 1,614 nucleotides, yielding a predicted translation product of 538 amino acids, in agreement with the estimated size of the purified protein analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The transcriptional start of pcpB was found to be 80 bp upstream of the translational start, and the transcript was found to be induced in Flavobacterium sp. strain ATCC 39723 by the presence of pentachlorophenol but to be constitutive in the Escherichia coli pcpB clone. DNA hybridizations with genomic DNAs from Arthrobacter sp. strain ATCC 33790 and Pseudomonas sp. strain SR3 revealed a similar-size 3.0-kb EcoRI fragment, whereas there was no positive hybridization with genomic DNA from Rhodococcus chlorophenolicus. Cell extracts from an E. coli pcpB overexpression strain, as well as the whole cells, were proficient in the dechlorination of pentachlorophenol to tetrachlorohydroquinone. Protein data base comparisons of the predicted translation products revealed regions of homology with other microbial monooxygenases, including phenol-2-monooxygenase and tryptophan-2-monooxygenase.

Amino Acid Sequence↗

PubMed1997

The action in vivo of glycine betaine in enhancement of tolerance of Synechococcus sp. strain PCC 7942 to low temperature.

The cyanobacterium Synechococcus sp. strain PCC 7942 was transformed with the codA gene for choline oxidase from Arthrobacter globiformis under the control of a constitutive promoter. This transformation allowed the cyanobacterial cells to accumulate glycine betaine at 60 to 80 mM in the cytoplasm. The transformed cells could grow at 20 degrees C, the temperature at which the growth of control cells was markedly suppressed. Photosynthesis of the transformed cells at 20 degrees C was more tolerant to light than that of the control cells. This was caused by the enhanced ability of the photosynthetic machinery in the transformed cells to recover from low-temperature photoinhibition. In darkness, photosynthesis of the transformed cells was more tolerant to low temperature such as 0 to 10 degrees C than that of the control cells. In parallel with the improvement in the ability of the transformed cells to tolerate low temperature, the lipid phase transition of plasma membranes from the liquid-crystalline state to the gel state shifted toward lower temperatures, although the level of unsaturation of the membrane lipids was unaffected by the transformation. These findings suggest that glycine betaine enhances the tolerance of photosynthesis to low temperature.

Alcohol Oxidoreductases↗

PubMed1999

Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases.

1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase (Qdo) from Pseudomonas putida 33/1 and 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (Hod) from Arthrobacter ilicis Rü61a catalyze an N-heterocyclic-ring cleavage reaction, generating N-formylanthranilate and N-acetylanthranilate, respectively, and carbon monoxide. Amino acid sequence comparisons between Qdo, Hod, and a number of proteins belonging to the alpha/beta hydrolase-fold superfamily of enzymes and analysis of the similarity between the predicted secondary structures of the 2,4-dioxygenases and the known secondary structure of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 strongly suggested that Qdo and Hod are structurally related to the alpha/beta hydrolase-fold enzymes. The residues S95 and H244 of Qdo were found to be arranged like the catalytic nucleophilic residue and the catalytic histidine, respectively, of the alpha/beta hydrolase-fold enzymes. Investigation of the potential functional significance of these and other residues of Qdo through site-directed mutagenesis supported the hypothesis that Qdo is structurally as well as functionally related to serine hydrolases, with S95 being a possible catalytic nucleophile and H244 being a possible catalytic base. A hypothetical reaction mechanism for Qdo-catalyzed 2,4-dioxygenolysis, involving formation of an ester bond between the catalytic serine residue and the carbonyl carbon of the substrate and subsequent dioxygenolysis of the covalently bound anionic intermediate, is discussed.

Amino Acid Sequence↗

PubMed1969

Selective inhibition of bacterial enzymes by free fatty acids.

Octanoic acid inhibits, in vitro, the bacterial enzymes glucose-6-phosphate dehydrogenase, phosphofructokinase, pyruvate kinase, fumarase, lactate dehydrogenase, and the malic enzyme of Arthrobacter crystallopoietes. The free fatty acid appears to act as an inhibitor of lipogenesis, although it does not affect the rate of gluconeogenesis. To demonstrate that this inhibition may be of physiological significance in vivo, those enzymes not involved in lipogenesis, such as fructose-1, 6-diphosphatase, phosphoglucomutase, phosphohexoisomerase, aconitase, nicotinamide adenine dinucleotide phosphate (NADP) isocitrate dehydrogenase, NADP glutamate dehydrogenase, malate dehydrogenase, and isocitrate lyase, were assayed and found not to be inhibited by the free fatty acid.

Arthrobacter↗

PubMed1975

Identification and flagellation of coryneform bacteria from poultry litter.

Thirth coryneform isolates from poultry litter were identified and checked for motility and flagellation. Twenty-seven formed a yellow pigment and 3 were orange. Twenty-three yellow strains were found to be Arthrobacter citreus, although starch was hydrolyzed by these strains. Four strains, including the three mainly pale yellow isolates, grew on citrate plus an ammonium salt and were classified as A. aurescens. Three orange strains were found to be Brevibacterium linens. Only six strains of A. citreus were motile. These strains displayed flagellated rods after 1 day and flagellated cocci after 5 days incubation. The flagellar shape and arrangement were studied. Non-motile strains never showed flagella after staining.

Actinomycetales↗

PubMed1976

Soybean flower-to-seed movement of epiphytic bacteria.

Epiphytic tracer bacteris (a Pseudomonas sp. and an Arthrobacter sp.) from soybean buds were introduced into open flowers of greenhouse-grown soybean plants. Of the 177 resulting pods cultured after surface disinfection, tracers were recovered from within 24. Seed from two of these pods also carried tracers.

Arthrobacter↗

PubMed1992

Bacteria that degrade p-chlorophenol isolated from a continuous culture system.

Two Gram-positive coryneform bacteria that degraded p-chlorophenol isolated from a continuous culture system are characterized. Isolate B (probably and Arthrobacter sp.) completely removed the p-chlorophenol from a medium with a concomitant increase in cell density within 16 h. Isolate F similarly removed the p-chlorophenol within 28 h but without an increase in cell density. Isolates B and F also removed the p-chlorophenol from a medium with p-chlorophenol as the sole carbon source within 32 and 48 h, respectively. The optimal temperature for p-chlorophenol degradation by both organisms was 25 to 30 degrees C. The optimal pH range for p-chlorophenol degradation was pH 7-9 for isolate B and pH 8-9 for isolate F. Since these native environmental bacteria can degrade p-chlorophenol, they may have an important application in waste water treatment processes.

Arthrobacter↗

PubMed1979

Structural homologies in alanine-rich acidic ribosomal proteins from procaryotes and eucaryotes.

The amino acid composition and amino-terminal sequence have been determined for the alanine-rich, acidic ribosomal 'A' protein (equivalent to Escherichia coli L7/L12) from three procaryotic cell types that live under extreme environmental conditions (Arthrobacter glacialis, Clostridium pasteurianum, and Bacillus stearothermophilus) as well as from wheat germ, a eucaryote source. These data are compared with previously published 'A' protein sequences from other procaryotes and eucaryotes. All the procaryotic 'A' proteins, with the exception of the very acidic 'A' protein from Halobacterium cutirubrum, show similar charge, size, and amino acid composition, as well as an extensive sequence homology in the N-terminal region. Some differences are observed between gram-negative and gram-positive bacteria. The 'A' proteins from eucaryotes contain two tyrosine molecules, an amino acid absent in procaryotic 'A' proteins, as well as a reduced number of valine residues and an increased amount of aspartic acid. The N-terminal sequence of wheat germ 'A' protein shows considerable homology with other eucaryotic 'A' proteins and also with H. cutirubrum. It also shows some sequence homology with E. coli 'A' proteins.

Alanine↗

PubMed1977

Studies of the glycine cleavage enzyme system in brain from infants with glycine encephalopathy.

Glycine content and enzyme activity of the glycine cleavage system were compared in autopsied brain from five infants dying with glycine encephalopathy and four control infants, including two with other types of hyperglycinemia. Glycine content was elevated 2- to 8-fold and glycine cleavage enzyme activity was undetectable in the brains of the glycine encephalopathy patients. Glycine content and enzyme activity were normal in the brains of the control patients, including one with ketotic hyperglycinemia secondary to methylmalonic acidemia. Prolonged dialysis failed to restore glycine cleavage enzyme activity in brain homogenates of glycine encephalopathy patients, and these homogenates failed to inhibit enzyme activity when added to homogenates of control brain. Radioactive bicarbonate was converted to radioactive glycine by control brain, but not by glycine encephalopathy brain. This finding, together with the results of recombination experiments between solubilized human brain enzymes and purified protein components of the bacterial glycine cleavage system of Arthrobacter globiformis, indicates that the enzyme defect in glycine encephalopathy involves at least the second or H protein of the 4-protein glycine cleavage enzyme system.

Amino Acid Metabolism, Inborn Errors↗

PubMed2005

Hypothesis: structures, evolution, and ancestor of glucose kinases in the hexokinase family.

Glucose kinase, which we tentatively use in this review, represents the enzymes catalyzing the phosphorylation of glucose and other hexoses by means of phosphoryl donors (ATP, ADP, and inorganic polyphosphate [poly(P)]). Except for glucose kinases utilizing ADP, all other glucose kinases belong to the hexokinase (HK) family and are classified into three groups based on primary structural information, i.e., groups HK, A, and B. The structural and evolutionary relationships of glucose kinases belonging to the above three groups have been controversial due to the lack of tertiary structural information on those in groups A and B. However, recent studies on the tertiary structures of poly(P)/ATP-glucomannokinase (GMK: a glucose kinase in group B) from Arthrobacter sp. strain KM and glucokinase (GK) (ecoGK: a glucose kinase in group A) from Escherichia coli have shed light on this problem. A comparison of the tertiary structures of GMK and ecoGK with those of glucose kinases in group HK demonstrated that both GMK and ecoGK are structurally homologous with glucose kinases in group HK, and that glucose kinases belonging to groups HK, A, and B in the HK family evolved divergently from a common ancestor. Based on the simple structure of GMK compared to those of ecoGK and glucose kinases in group HK, and the putative poly(P)-binding site in GMK, we propose that the ancestor of glucose kinases in the HK family was similar to GMK and used poly(P). We also discuss the ancestor and evolutionary process of ROK proteins, whose primary structures are homologous with those of glucose kinases in group B, in connection with the ancestor and evolutionary process of glucose kinases in the HK family.

Amino Acid Sequence↗

PubMed1996

Biodegradability of oxidized poly(vinyl alcohol).

Poly(vinyl alcohol) dehydrogenase (PVADH) purified from Pseudomonas sp. 113P3 catalyzed an oxidation of poly(vinyl alcohol) (PVA) in the presence of pyrroloquinoline quinone (PQQ) to give a beta-diketone structure on PVA. Although PVADH oxidized not only enzymatically oxidized PVA but also chemically oxidized PVA, PVA-degrading microorganisms, Pseudomonas sp. 113P3 and Arthrobacter tumescens sp. 52-1 grew on the enzymatically oxidized PVA, but not on the chemically oxidized PVA. This suggests that the growth of PVA-degrading microorganisms is affected by the structure of oxidized PVA.

Alcohol Oxidoreductases↗

PubMed2000

Enzymatic assay of histamine by amperometric detection of H2O2 with a peroxidase-based sensor.

A method for an enzymatic assay of histamine by using histamine oxidase from Arthrobacter globiformis in combination with amperometric determination of H2O2 is described. Histamine could be quantified at a level as low as 10(-7) M. The assay is adaptable to determine histamine in food samples including tuna fish with good sensitivity and selectivity.

Amine Oxidase (Copper-Containing)↗

PubMed2002

Novel reversible indole-3-carboxylate decarboxylase catalyzing nonoxidative decarboxylation.

After enrichment culture with indole-3-carboxylate in static culture, a novel reversible decarboxylase, indole-3-carboxylate decarboxylase, was found in Arthrobacter nicotianae FI1612 and several molds. The enzyme reaction was examined in resting-cell reactions with A. nicotianae FI1612. The enzyme activity was induced specifically by indole-3-carboxylate, but not by indole. The indole-3-carboxylate decarboxylase of A. nicotianae FI1612 catalyzed the nonoxidative decarboxylation of indole-3-carboxylate into indole, and efficiently carboxylated indole and 2-methylindole by the reverse reaction. In the presence of 1 mM dithiothreitol, 50 mM Na2 S2O3, and 20% (v/v) glycerol, indole-3-carboxylate decarboxylase was partially purified from A. nicotianae FI1612. The purified enzyme had a molecular mass of approximately 258 kDa. The enzyme did not need any cofactor for the decarboxylating and carboxylating reactions.

Arthrobacter↗

PubMed2003

Inhibition of beta-fructofuranosidases and alpha-glucosidases by synthetic thio-fructofuranoside.

A synthetic beta-thio-fructofuranoside of mercaptoethanol inhibited not only beta-fructofuranosidases but also alpha-glucosidases. The compound was hardly hydrolyzed by the glycosidases. The thio-fructoside competitively inhibited beta-fructofuranosidases from Aspergillus niger, Candida sp., and Saccharomyces cerevisiae, but not Arthrobacter beta-fructofuranosidase at all. Sucrase activity of rat intestinal sucrase/isomaltase complex was also suppressed in the presence of the thio-fructoside. The thio-fructoside showed noncompetitive inhibition toward maltase activity of the rat intestinal enzyme complex and Saccharomyces sp. alpha-glucosidase. Inhibition against the Bacillus stearothermophilus alpha-glucosidase, Rhizopus glucoamylase, and porcine kidney trehalase were more slight than that against these two alpha-glucosidases.

Animals↗

PubMed2004

Isolation of a cadmium-releasing bacterium and characterization of its novel protease.

Microorganisms were screened for their ability to release cadmium from scallop hepatopancreas, which is the main residue after removing of the edible parts of scallop. The isolated strain, 23-0-11, identified as Arthrobacter nicotinovorans, secreted a protease which released cadmium from scallop hepatopancreas into the liquid medium. The molecular mass of the enzyme was estimated to be 27 kDa. The sequence of the 15 N-terminal amino acids of the protease showed no close similarity with any other protein. Compared with a commercial enzyme, the purified protease had greater ability to release cadmium. The enzyme activity was greatest at 50 degrees C and pH 7.0, and was enhanced in the presence of Ca(2+), Mg(2+) and Mn(2+), while being strongly inhibited by Co(2+). The inhibition profile by the serine protease inhibitor, phenylmethylsulphonyl fluoride (PMSF), confirmed that the protease belonged to the serine protease family.

Animals↗

PubMed1983

Quantitation of immunoadsorbed flavoprotein oxidases by luminol-mediated chemiluminescence.

The detection of the flavoenzymes 6-hydroxy-L-nicotine oxidase and 6-hydroxy-D-nicotine oxidase at the sub-femtomol level was achieved by coupling the reaction of the immunoadsorbed proteins to the peroxidase-catalysed oxidation of luminol. The H2O2-producing oxidases retained their full activity when bound to the respective immobilized antibodies. This fact allowed the concentration of the enzymes from very dilute solutions and the quantitative assay of their activities in the microU range. Due to strict stereoselectivity and the absence of immunological cross-reactivity, the two flavoproteins could be determined in the same solution. This method was used to measure the 6-hydroxy-D-nicotine oxidase and 6-hydroxy-L-nicotine oxidase activities in Escherichia coli RR1 and different Arthrobacter strains cultured under non-inducing conditions. The same activity ratio of 6-hydroxy-L-nicotine oxidase/6-hydroxy-D-nicotine oxidase as in D L-nicotine-induced cells of A. oxidans was observed in non-induced wild type and in riboflavin-requiring (rf-) mutant cells of this aerob.

Antigen-Antibody Complex↗

PubMed2004

Does smearing inoculum reflect the bacterial composition of the smear at the end of the ripening of a French soft, red-smear cheese?

The microbial community composition and dynamics during the production of a French soft, red-smear cheese were investigated. The colonization efficiency of the smearing inoculum was followed, and the parts played by the inoculum used and the resident microflora were tentatively estimated. Single-strand conformation polymorphism analysis (SSCP) was applied to 2 productions of a soft, red-smear cheese produced by the same dairy plant at 4-mo intervals. Microbial composition of the different cheese samples analyzed was found to be reproducible from one production to another. However, the composition of the surface flora of both cheeses at the end of the ripening did not reflect the composition of the smearing inoculum used, qualitatively as well as quantitatively. These results were confirmed by those obtained when assessing the microbial composition of the culturable flora by the spread plate technique. The inoculum used by the industry had low resiliency potentialities against colonization of cheeses by resident organisms. Therefore, fitness and colonization potential of smearing inocula should be carefully assessed by the industry before use. The use of Arthrobacter strains as part of the smearing inoculum should be evaluated.

Arthrobacter↗

PubMed1982

Structural features of cytochalasins responsible for gram-positive bacterial inhibitions.

A study of the relative effectiveness of some eighteen natural and synthetically modified cytochalasins on the uptake of glucose by the Gram-positive bacterium Arthrobacter sialophilus showed that cytochalasins B, C or D and aspochalasins A, C or D were inactive natural congeners. The presence of an alpha,beta-unsaturated carbonyl group in the macrolide moiety of these compounds with appropriate bioisosteric placement, as exemplified by cytochalasin A and aspochalasin B, are requisite molecular features. The transmembrane inhibitory index of active compounds was enhanced by increasing their lipophilicity. Thiol adducts of CA were around 20% as active in solute uptake inhibition as was the free drug. Radioactive 7-O-acetyl CA and its thiol adduct were each rapidly taken up by A. sialophilus and remained firmly bound to cellular components even after denaturant manipulations. These findings provide strong evidence for a stable association between CA and presumptive macromolecular receptors in transport and related processes.

Arthrobacter↗