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PubMed1974

Biosynthesis of carotenoids in Brevibacterium sp. KY-4313.

The biosynthesis of 4-keto and 4,4'-diketo carotenoids in Brevibacterium sp. KY-4313 was studied. Echinenone and canthaxanthin were isolated from the cultures grown on a medium containing several n-alkanes. When glutathione was added to the bacterial cultures, the formation of canthaxanthin was inhibited while beta-carotene and its hydroxy derivatives accumulated. It is suggested that these 4-hydroxy compounds, isocryptoxanthin, isozeaxanthin, and 4-hydroxy-4'-keto-beta-carotene, are intermediates in the biosynthesis of canthaxanthin. In the presence of 2-(4-chlorophenylthio)-triethylamine hydrochloride or nicotine, lycopene and neurosporene accumulated. The beta-carotene level decreased slightly but beta-zeacarotene remained unchanged. beta-carotene and its derivatives were resynthesized upon removal of the inhibitors. It was concluded that cyclization can take place at either the neurosporene or lycopene level in Brevibacterium sp. KY-4313.

Brevibacterium↗
PubMed1990

Purification, cloning, and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: structural evidence for genetic coupling with nitrile hydratase.

An enantiomer-selective amidase active on several 2-aryl and 2-aryloxy propionamides was identified and purified from Brevibacterium sp. strain R312. Oligonucleotide probes were designed from limited peptide sequence information and were used to clone the corresponding gene, named amdA. Highly significant homologies were found at the amino acid level between the deduced sequence of the enantiomer-selective amidase and the sequences of known amidases such as indoleacetamide hydrolases from Pseudomonas syringae and Agrobacterium tumefaciens and acetamidase from Aspergillus nidulans. Moreover, amdA is found in the same orientation and only 73 bp upstream from the gene coding for nitrile hydratase, strongly suggesting that both genes are part of the same operon. Our results also showed that Rhodococcus sp. strain N-774 and Brevibacterium sp. strain R312 are probably identical, or at least very similar, microorganisms. The characterized amidase is an apparent homodimer of Mr 2 x 54,671 which exhibited under our conditions a specific activity of about 13 to 17 mumol of 2-(4-hydroxyphenoxy)propionic R acid formed per min per mg of enzyme from the racemic amide. Large amounts of an active recombinant enzyme could be produced in Escherichia coli at 30 degrees C under the control of an E. coli promoter and ribosome-binding site.

Amides↗
PubMed1994

Degradation of fluorene by Brevibacterium sp. strain DPO 1361: a novel C-C bond cleavage mechanism via 1,10-dihydro-1,10-dihydroxyfluoren-9-one.

Angular dioxygenation has been established as the crucial step in dibenzofuran degradation by Brevibacterium sp. strain DPO 1361 (V. Strubel, K. H. Engesser, P. Fischer, and H.-J. Knackmuss, J. Bacteriol. 173:1932-1937, 1991). The same strain utilizes biphenyl and fluorene as sole sources of carbon and energy. The fluorene degradation sequence is proposed to be initiated by oxidation of the fluorene methylene group to 9-fluorenol. Cells grown on fluorene exhibit pronounced 9-fluorenol dehydrogenase activity. Angular dioxygenation of the 9-fluorenone thus formed yields 1,10-dihydro-1,10-dihydroxyfluoren-9-one (DDF). A mechanistic model is presented for the subsequent C-C bond cleavage by an NAD(+)-dependent DDF dehydrogenase, acting on the angular dihydrodiol. This enzyme was purified and characterized as a tetramer of four identical 40-kDa subunits. The following Km values were determined: 13 microM for DDF and 65 microM for 2,3-dihydro-2,3-dihydroxybiphenyl. The enzyme also catalyzes the production of 3-(2'-carboxyphenyl)catechol, which was isolated, and structurally characterized, in the form of the corresponding lactone, 4-hydroxydibenzo-(b,d)-pyran-6-one. Stoichiometry analysis unequivocally demonstrates that angular dioxygenation constitutes the principal pathway in Brevibacterium sp. strain DPO 1361.

Alcohol Oxidoreductases↗
PubMed1961

Taxonomically significant color reactions of Brevibacterium linens.

Grecz, Nicholas (University of Chicago, Chicago, Ill.), and Gail M. Dack. Taxonomically significant color reactions of Brevibacterium linens. J. Bacteriol. 82:241-246. 1961.-Brevibacterium linens was observed to give characteristic color reactions with certain bases and acids. An intensive carmine-red color appeared immediately after addition of a drop of 5 n sodium hydroxide, 5 n potassium hydroxide, and saturated barium hydroxide. A light carmine-red was given by lithium hydroxide, and a light orange-red with a milky suspension of calcium hydroxide. No discernible color change was given with weak bases such as ammonium hydroxide, aniline, and pyridine.A characteristic salmon-pink color was produced when B. linens was rubbed with a glass rod in a drop of glacial acetic acid or filter paper; a brick-red color was produced with aniline under these conditions. With syrupy phosphoric acid a green color appeared within 3 to 4 min which turned blue after approximately 3 hr. The blue color was stable for several days. On the basis of these color reactions, B. linens could be distinguished from other microorganisms possessing yellow-orange pigmentation, i.e., Staphylococcus aureus, Staphylococcus epidermidis, Micrococcus flavus, Micrococcus citreus, Mycobacterium phlei, Sarcina lutea. Therefore, these color changes may be used for the identification of B. linens. Original isolates of B. linens from cheese were tested by these spot reactions and all presumptive identifications could be subsequently confirmed by conventional methods. Blue and green colors appeared in all yellow-orange chromogens treated with sulfuric, perchloric, and hydrochloric acids and hence these colors were not specific for B. linens.

Brevibacterium↗
PubMed1962

Occurrence of nucleotides in culture fluids of microorganisms. III. Nucleotide excretion by Brevibacterium liquefaciens sp. n. with special reference to uridine diphospho-N-acetylglucosamine compounds.

Okabayashi, T. (Shionogi Research Laboratory, Fukushimaku, Osaka, Japan). Occurrence of nucleotides in culture fluids of microorganisms. III. Nucleotide excretion by Brevibacterium liquefaciens sp. n. with special reference to uridine diphospho-N-acetylglucosamine compounds. J. Bacteriol. 84:1-8. 1962.-Among various nucleotides excreted in the culture broth of Brevibacterium liquefaciens sp. n., four uridine nucleotides containing N-acetylglucosamine were isolated. These were found to be uridine diphospho-N-acetylglucosamine and Park's compounds 1, 2, and 3. The significance of the appearance of these cell-wall precursors in the culture fluid of B. liquefaciens is discussed.

Acetylglucosamine↗
PubMed1967

Formation of adenosine cyclic 3',5'-phosphate by nonproliferating cells and cell-free extract of Brevibacterium liquefaciens.

The formation of adenosine cyclic 3',5'-phosphate by Brevibacterium liquefaciens ATCC 14929 was studied with the use of nonproliferating cells and cell-free extract. With nonproliferating cells provided by deprivation of sulfate, the formation of this nucleotide was accelerated by adding some amino acids and sugars. Among amino acids tested, alanine and asparagine were most effective. Pentoses were more favorable than hexoses and other sugars. Formation of adenosine cyclic 3',5'-phosphate was observed also with chloramphenicol-treated cells. Experiments on cell-free extract showed that addition of alanine or pyruvate stimulated the formation of adenosine cyclic 3',5'-phosphate from adenosine-5'-triphosphate. When alanine was added to the cell-free system, shaking of the reaction mixture further increased the amount of the nucleotide, but pyruvate was far more effective than alanine. No synergistic effect of alanine and pyruvate was observed. Some enzyme activity was observed which decomposed adenosine cyclic 3',5'-phosphate, but it was weak as compared with adenyl cyclase activity in the presence of pyruvate. From the results obtained, it appears that pyruvate may act as an activating factor of adenyl cyclase in Brevibacterium liquefaciens.

Adenine Nucleotides↗
PubMed1994

Differentiation of Brevibacterium spp. encountered in clinical specimens.

Forty-three strains belonging to the genus Brevibacterium which were encountered in clinical materials over 2 decades were compared with reference strains, including the type strains, of B. casei, B. epidermidis, B. mcbrellneri, B. iodinum, and B. linens. By means of carbohydrate assimilation tests (CATs) the 43 clinical isolates could be assigned to the species B. casei (n = 41) and B. epidermidis (n = 2). DNA-DNA hybridizations were performed for 20 clinical isolates and confirmed the species identification of the isolates. Cellular fatty acid profiles of all strains were determined and found to have less discriminative power than CATs. This is the first report indicating that most clinical Brevibacterium isolates are B. casei and that CATs provide an easy-to-perform method for species determination within the genus, thus avoiding nucleic acid techniques.

Brevibacterium↗
PubMed2000

Brevibacterium casei sepsis in an 18-year-old female with AIDS.

Brevibacterium sp. was isolated from the blood of an acutely ill 18-year-old female with AIDS. The isolate was identified as Brevibacterium casei by use of carbohydrate assimilation tests. Treatment was successful with intravenously administered ciprofloxacin. To our knowledge, this is the first report of sepsis caused by B. casei in a human immunodeficiency virus-infected patient.

AIDS-Related Opportunistic Infections↗
PubMed2002

Bacteremia caused by Brevibacterium species in a patient with chronic lymphocytic leukemia.

We report a case of bacteremia caused by Brevibacterium species which is one of the coryneform bacteria, in a patient with chronic lymphocytic leukemia. We conclude that, if a coryneform bacteria is isolated from sterile body sites, it must be carefully evaluated, and especially in immunocompromised patients, Brevibacterium species should be considered as potential pathogens.

Bacteremia↗
PubMed1996

Molecular cloning of a novel gene, dtsR, which rescues the detergent sensitivity of a mutant derived from Brevibacterium lactofermentum.

Several strains of Corynebacterium and Brevibacterium are known for their ability to secrete large amounts of amino acids, especially L-glutamate. We focused on the mechanism of L-glutamate secretion triggered by a detergent, namely polyoxyethylenesorbitan monopalmitate (PESP). A mutant strain, AJ11060, derived from Brevibacterium lactofermentum ATCC 13869 indicates the sensitivity to PESP. A multicopy suppresser gene that compliments the sensitivity of AJ11060 to the detergent was derived from a gene library of B. lactofermentum AJ12036. A 2855-bp DNA fragment was cloned and sequenced. An open reading frame was found that coded for the rescuer gene of the sensitivity to PESP of AJ11060 and was designated dtsR. The expression of the dtsR gene in B. lactofermentum was confirmed by using anti-DtsR antibody. The deduced DtsR protein indicated significant homology with some biotin enzymes such as the beta chain of propionyl-CoA carboxylase from rat (48.3%) and human (48.7%), or a 12S chain of methylmalonyl-CoA carboxyltransferase from Propionibacterium freudenreichii (43.1%).

Amino Acid Sequence↗
PubMedDate not supplied

Production of hydrogen sulphide in milkfat-coated microcapsules containing Brevibacterium linens and cysteine.

Milkfat-coated microcapsules containing Brevibacterium linens and cysteine were used to produce hydrogen sulphide, one of Cheddar cheese flavour compounds. Hydrogen sulphide production was substantially reduced and delayed in the encapsulated system as compared with that of the unencapsulated system. Hydrogen sulphide was not produced aerobically whereas substantial amounts of hydrogen sulphide were produced in a nitrogen purged system. The inhibitory effect of the initial aerobic condition disappeared after 8 days of incubation. In spite of the lag in hydrogen sulphide production under aerobic conditions almost the same amount of hydrogen sulphide was produced in oxygen purged samples as in the nitrogen purged samples after 10 days of incubation. Moderate heat treatment (2 min at 58 degrees C) of cell suspension-milkfat-emulsion increased subsequent hydrogen sulphide production. The optimum pH and temperature for hydrogen sulphide production from cysteine by Brevibacterium linens were 6 degrees C and 32 degrees C, respectively. Antioxidants BHT, BHA and ascorbic acid had negligible effects on production of hydrogen sulphide in the encapsulated system.

Animals↗
PubMed1993

Genomic organization of the biotin biosynthetic genes of coryneform bacteria: cloning and sequencing of the bioA-bioD genes from Brevibacterium flavum.

Three coryneform bacteria, Brevibacterium flavum, Brevibacterium lactofermentum and Corynebacterium glutamicum have been shown to be able to convert 7-keto-8-aminopelargonic acid to biotin through a biotin synthetic pathway identical to that from Escherichia coli (Hatakeyama et al., DNA Sequence, in press, 1993). We report in this paper the cloning and sequencing of the biotin biosynthetic genes encoding the 7,8-diaminopelargonic acid aminotransferase (bioA) and the dethiobiotin synthetase (bioD) of B. flavum MJ233, by complementation of E. coli bioA and bioD mutants. Both bioA and bioD genes from B. flavum were located on a 4.0-kb SalI DNA fragment. Nucleotide sequence analysis of this fragment revealed that these genes consist of a 1272 bp and a 675 bp open reading frame, respectively. The deduced amino acid sequence of the 7,8-diaminopelargonic acid aminotransferase (BioA) is 51.3% and 31.9% identical to that of the E. coli and Bacillus spaericus bioA gene products, respectively. The deduced amino acid sequence of the dethiobiotin synthetase (BioD) is 25.9% and 32.7% identical to that of the E. coli and B. sphaericus bioD gene products, respectively. In addition, the genomic organization of the bioA, bioB and bioD genes in B. flavum has been shown to be different from that in E. coli and B. sphaericus.

Amino Acid Sequence↗
PubMed1993

Analysis of the biotin biosynthesis pathway in coryneform bacteria: cloning and sequencing of the bioB gene from Brevibacterium flavum.

The biotin biosynthetic pathway of three coryneform bacteria, Brevibacterium flavum, Brevibacterium lactofermentum, and Corynebacterium glutamicum were analysed by cross-feeding experiments using several Escherichia coli biotin-requiring mutants. The three strains of coryneform bacteria tested were able to convert 7-keto-8-aminopelargonic acid to biotin, through a biotin synthetic pathway identical to that from E. coli. The biotin biosynthetic gene, bioB, of B. flavum was cloned by phenotypic complementation of E. coli bioB mutants. The bioB gene was located on a 1.7 kb HindIII-SacI DNA fragment. Nucleotide sequence analysis of this fragment revealed that the bioB gene of B. flavum consists of a 1005 bp open reading frame. Its deduced amino acid sequence is 35.7% and 31.5% identical to that of the E. coli and Bacillus sphaericus bioB gene products, respectively. B. flavum mutants obtained by in vivo disruption of the bioB gene lost their ability to grow on minimal medium containing dethiobiotin, indicating that the bioB gene product is necessary for the conversion of dethiobiotin to biotin.

Amino Acid Sequence↗
PubMed2001

[Biodegradation of polycyclic aromatic hydrocarbons by a preponderant brevibacterium].

A preponderant brevibacterium was isolated from the sludge contaminated by coke-plantwaste water for a long time. The bacterium was effective on the degradation and transformation of anthracene, phenanthrene and pyrene. The degradation process can be accelerated by ferric ions. 10 hours after aeration, the removing rates of anthracene, phenanthrene and pyrene by the brevibacterium were about 75%, 87% and 62% respectively. 106 hours after aeration, the removing rates of total organic carbon (TOC) caused by anthracene, phenanthrene and pyrene were 50%, 90%, and 50% respectively.

Aerobiosis↗
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↗
PubMed1998

New shuttle vectors for Rhodococcus sp. R312 (formerly Brevibacterium sp. R312), a nitrile hydratase producing strain.

Two shuttle vectors named pRC52 (10.7 Kb) and pRK52 (12.2 Kb) carrying chloramphenicol (Cm) and chloramphenicol plus kanamycin (Km) resistance genes, respectively, were constructed by fusion of a cryptic plasmid pBL13869 (replicon pBL1, 5.8 Kb) from Brevibacterium lactofermentum ATCC13869 with pBR328 E. coli plasmid. Transformation of Rhodococcus sp. R312 (formerly Brevibacterium sp. R312) protoplasts was realised with an efficiency of 28 transformants per micrograms of DNA.

Brevibacterium↗
PubMed1988

Isolation and preliminary characterization of twenty bacteriophages infecting either brevibacterium or arthrobacter strains.

Thirty-seven bacteriophages plaquing on Corynebacterium, Brevibacterium, or Arthrobacter strains were isolated from soil or vegetation samples. Restriction analysis of phage DNA indicated that 20 phages were unique; one of them produced entirely turbid plaques on Brevibacterium ketoglutamicum and was characterized as temperate. All these phages were assigned to group B of the classification of Bradley (Bacteriol. Rev. 31:230-314, 1967) and had relatively narrow host ranges.

Journal Article↗
PubMed1998

Intracellular changes in ions and organic solutes in halotolerant brevibacterium sp. Strain JCM 6894 after exposure to hyperosmotic shock

In the present study we aimed to observe the intracellular responses when there was a hyperosmotic shock with a large shift in ionic strength in nutrient-rich and nutrient-poor external environments in order to clarify the availability of substrates. To do this, we used the halotolerant organism Brevibacterium sp. strain JCM 6894, which is able to grow in the presence of a wide range of salt concentrations. Hyperosmotic shock was induced by transferring cells in the late exponential phase of growth in a complex medium containing 0.5 M NaCl into either old or fresh culture medium containing 2 M NaCl. Changes in the growth rate, in the pH of the medium, and in the internal cation or organic solute concentrations in the cytosol after an upshock were analyzed as a function of incubation time. The cells exhibited very different responses to upshocks in fresh culture medium and in old culture medium; in fresh culture medium, growth was stimulated and the medium became more acidic, whereas the old culture medium repressed growth and the medium became more alkaline. The intracellular free Na+ concentrations remained low (80 nmol mg of protein-1) after an upshock in fresh culture medium, although they quickly increased twofold in the old culture medium. In contrast, K+ ions immediately accumulated in the cells in fresh culture medium, whereas K+ ions were taken up quite slowly in old culture medium. Furthermore, the cells placed in fresh culture medium transiently accumulated alanine and glutamine in response to the upshock, but the cells placed in old culture medium did not. Growth of the Brevibacterium strain at higher levels of salinity was supported by ectoine synthesis but was not observed after the shift to high-osmolarity conditions in the old culture. In the fresh culture, however, ectoine was vigorously synthesized in cells for more than 5 h after the upshock; the concentration of ectoine in cells was more than 3,500 nmol mg of protein-1 at 10 h, which corresponded to a ninefold increase compared to the concentration before the shock. These findings are consistent with the results of an analysis of the extracellular medium composition before and after the upshock.

Journal Article↗