Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Brevibacterium”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 91 records · Page 5Linked to original sources
PubMed2026

Whole-genome analysis of Brevibacterium sanguinis AZMABM HM27: a bacterial isolate from the sea anemone Radianthus magnifica and exhibiting promising multi-therapeutic properties.

BACKGROUND: The marine anemone Radianthus magnifica harbors symbiotic microbes with promising biomedical potential, yet their diversity and therapeutic properties remain underexplored. This study aimed to characterize a symbiotic bacterium isolated from R. magnifica collected from Samalona Island, Indonesia, and to evaluate its multi-therapeutic potential. METHODS: Strain AZMABM HM27 was characterized using whole-genome sequencing, functional annotation, biosynthetic gene cluster prediction, molecular docking, and in vitro bioactivity assays. RESULTS: Phylogenetic and genome-based analyses confirmed AZMABM HM27 as Brevibacterium sanguinis, with an OrthoANI value of 97.37% and a dDDH value of 76.50% against the type strain. The genome comprises a 3,834,082 bp chromosome encoding 3,362 protein-coding genes, including 95 genes involved in secondary metabolite biosynthesis. Five biosynthetic gene clusters were predicted, including those associated with ectoine, terpene, and siderophore production. The crude extract demonstrated antioxidant activity (IC₅₀ = 0.87 mg/mL), anti-inflammatory activity (up to 60% inhibition), antidiabetic activity through α-glucosidase inhibition (up to 40% inhibition), and dose-dependent antiproliferative activity against MCF-7 breast cancer cells (74.10% viability at 1 mg/mL). Molecular docking identified a lead compound, 8,9,9,10,10,11-hexafluoro-4,4-dimethyl-3,5-dioxatetracyclo [5.4.1.0(2,6)0.0(8,11)] dodecane, with strong binding affinities to selected therapeutic targets. CONCLUSIONS: B. sanguinis AZMABM HM27 represents a marine symbiotic strain associated with R. magnifica and a promising source of bioactive compounds with antioxidant, anti-inflammatory, antidiabetic, and antiproliferative potential. Further purification, structural elucidation, and in vivo studies are warranted to validate its therapeutic potential.

Animals↗
PubMed1975

Comparison of batch and semicontinuous cultures for production of protein from mesquite wood by Brevibacterium sp. JM98A.

The production of protein by a Brevibacterium sp. JM98A using mesquite wood as the substrate was compared in batch and semicontinuous cultures. A 14 liter glass fermentor with automatic pH, temperature, and foam control was used for the study. A pH range of 6.6 to 7.2 was optimum for the growth of JM98A. The batch and semicontinuous cultures were compared on the basis of viable cell counts, protein production, CMC-Ase (beta-1,4-glucanase) activity, and filter paper cellulase (beta-1,4-glucan cellobiohydrolyase) activity. Total hexose, cellulose, and reducing sugar consumption were measured. The semicontinuous process yielded 2.97 times as much protein in 72 hr as the batch cultures. Most of the biomass resulted from the utilization of soluble sugars rather than from the degradation of cellulose during the semicontinuous process.

Bacteriological Techniques↗
PubMed1979

Continuous production of NADP by immobilized Brevibacterium ammoniagenes cells.

Whole cells of Brevibacterium ammoniagenes IAM 1645 having the polyphosphate NAD-kinase were successfully immobilized in a polyacrylamide gel lattice. The immobilized cells were activated by treatment with organic solvents or detergents. The pH optimum of the immobilized cells for the production of NADP was 7.0, and divalent metal ions were required to maintain the elevated activity of polyphosphate NAD-kinase. Highly pure NADP was continuously produced in high yield by the immobilized cell column. The half-life of this column was about eight days.

Brevibacterium↗
PubMed1989

Purification and properties of the beta-glucosidase from a nitrile hydratase-producing Brevibacterium sp. strain R312.

Besides its nitrile hydratase and wide spectrum amidase activities, the Brevibacterium sp. R312 strain also possesses a constitutive beta-glucosidase. Its optimum pH is 6. The enzyme was purified by fractionation precipitation with ammonium sulfate followed by chromatographic elutions on Q-Sepharose Fast Flow, Sephadex G-200 and Phenyl Superose. The resulting purification was 1960 folds for a 6% yield. The molecular weight of this enzyme was estimated at 180,000. It contains two identical sub-units. The pI is 5.5. This enzyme has a strong affinity for aryl-beta-glycosides:pNPG, prunassine; it could also degrade linamarine. It is inhibited by p-chloromercuribenzoate, delta-gluconolactone and glucose.

Brevibacterium↗
PubMed1993

Separate enzymes catalyze the final two steps of coenzyme A biosynthesis in Brevibacterium ammoniagenes: purification of pantetheine phosphate adenylyltransferase.

We have discovered that the final two steps in coenzyme A biosynthesis in Brevibacterium ammoniagenes are catalyzed by distinct enzymes, readily separated by DEAE sepharose anion exchange chromatography. This is in contrast to mammalian tissues in which these two reactions are catalyzed by a single bifunctional enzyme (Worrall, D.M., and Tubbs, P.K. (1983) Biochem. J. 215, 153-157) and Bakers yeast in which these two activities have been identified as part of a multifunctional complex (Bucovaz, E.T., Rhoades, J.L., and Tarnowski, S.J. (1980) Fed. Proc. 39 (6), 142). The pantetheine phosphate adenylyltransferase has been purified to homogeneity and found to exist as a trimeric protein of molecular mass approximately 108 kDa. Of other nucleoside triphosphates tested as substrates, only 2'-deoxy-ATP showed measurable activity, being 27% that of ATP.

Brevibacterium↗
PubMed1995

The isomerization catalyzed by Brevibacterium sterolicum cholesterol oxidase proceeds stereospecifically with one base.

We have demonstrated that the isomerization reaction catalyzed by Brevibacterium sterolicum (ATCC 81387) cholesterol oxidase (EC 1.1.3.6) proceeds via a stereospecific proton transfer from the 4 beta carbon to the 6 beta carbon to form 4-cholestene-3-one using deuterated and nondueterated substrates. This result implies that there is one active site base, positioned over the beta-face, responsible for isomerization. On the basis of X-ray crystallographic evidence [Li, J., Vrielink, A., Brick, P. & Blow, D. M. Biochemistry 32, 11507-11515 (1993)], glutamate-361 is the most likely candidate for this general base.

Brevibacterium↗
PubMed1997

A dtsR gene-disrupted mutant of Brevibacterium lactofermentum requires fatty acids for growth and efficiently produces L-glutamate in the presence of an excess of biotin.

A dtsR gene encoding a homolog of the beta subunit of some biotin-containing enzymes suppresses a detergent-sensitive mutation of Brevibacterium lactofermentum (E. Kimura et al., 1996, Biosci. Biotech. Biochem. 60, 1565-1570), which has been used for the fermentative production of L-glutamate. When the dtsR gene was disrupted, the organism exhibited strict fatty acid auxotrophy; oleate or oleate ester, but not palmitate ester or stearate ester, supported the growth of the delta dtsR mutant. Immunoblotting with an anti-DtsR antibody revealed that no intact DtsR was present in the cytosol of the delta dtsR mutant. In the presence of an excess of biotin, the wild type strain did not produce L-glutamate whereas the delta dtsR mutant efficiently produced it. The mechanism underlying the efficient production of L-glutamate by the delta dtsR mutant is discussed as to the possible role of dtsR in fatty acid metabolism.

Bacterial Proteins↗
PubMed1994

Preliminary crystallographic study of protocatechuate 3,4-dioxygenase from Brevibacterium fuscum.

The enzyme protocatechuate 3,4-dioxygenase from the Gram positive organism Brevibacterium fuscum crystallizes in the triclinic space group P1 with unit cell dimensions a = 96.1 A, b = 97.2 A, c = 118.1 A and alpha = 113.9 degrees, beta = 90.7 degrees, gamma = 117.8 degrees. The rod-like crystals diffract to 2.4 A resolution. Rotation function analysis suggests that there are six promoters arranged with local 32 symmetry in the asymmetric unit rather than the previously proposed pentameric complex.

Brevibacterium↗
PubMedDate not supplied

Crystallization and preliminary X-ray analysis of cholesterol oxidase from Brevibacterium sterolicum containing covalently bound FAD.

Single crystals of cholesterol oxidase from Brevibacterium sterolicum containing a covalently bound form of the FAD cofactor have been obtained. The crystals are grown by vapor diffusion using the hanging drop technique from 12% polyethylene glycol, Mr 8000, and 75 mM MnSO4 as the precipitant at pH 5.2. In order to obtain large diffraction quality crystals, nucleation must occur at 22 degrees C with subsequent growth at 17 degrees C. The crystals belong to the monoclinic space group P21 with cell dimensions a = 78. 5 A, b = 126.7 A, c = 82.4 A and beta = 108.9 degrees with two protein molecules per asymmetric unit. Diffraction of these crystals has been observed to at least 2.2 A resolution and they are suitable for an X-ray structure analysis.

Amino Acid Sequence↗
PubMed1996

A Brevibacterium linens pRBL1 replicon functional in Corynebacterium glutamicum.

Brevibacterium linens RBL strain cryptic plasmid pRBL1 (8.0 kb) is described. A region involved in pRBL1 autonomous replication in Corynebacterium glutamicum was identified by insertion and deletion mapping and partially sequenced. This region encodes for a hypothetical 310-amino acid (aa) protein closely related to the replicases of plasmids pXZ10142 (C. glutamicum) and pAL5000 (Mycobacterium fortuitum). The 310-aa protein also shows significant homology to proteins of pColE5-099 (Shigella sonnei) and pJD1 (Neisseria gonorrhoea). At least one of these proteins, the Rep protein of pColE5-099, is known to be involved in theta replication.

Amino Acid Sequence↗
PubMed1996

A cryptic plasmid pBL1 from Brevibacterium lactofermentum causes growth inhibition and filamentation in Escherichia coli.

A shuttle vector composed of pBL1, a 4.46-kb cryptic plasmid from coryneform bacterium Brevibacterium lactofermentum, and Escherichia coli vector pHSG298 was found to inhibit growth and cause cell filamentation in E coli. After construction of several deletions of pBL1, a 1.23-kb AccI-HindIII fragment was found responsible. DNA sequence analysis showed that this fragment contained a 726-bp-long open reading frame (ORF3), encoding a protein with 242 amino acid residues. Corresponding to ORF3, a 28-kDa protein was detected in an in vitro protein synthesis system. ORF3 was dispensable for the stable maintenance of pBL1 in coryneform bacteria.

Brevibacterium↗
PubMed1997

Cloning, overexpression, and mutagenesis of the gene for homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum.

Homoprotocatechuate (hpca, 3,4-dihydroxyphenylacetate) is a central intermediate for the bacterial degradation of aromatic compounds. Homoprotocatechuate 2,3-dioxygenase (HPCD) catalyzes the key ring cleavage step in the metabolism of hpca by the Gram (+) bacterium Brevibacterium fuscum to yield alpha-hydroxy-delta-carboxymethyl cis-muconic semialdehyde. A genomic DNA library of B. fuscum was constructed in Escherichia coli using a cosmid vector and screened by spraying the cells with hpca. One clone was found to contain the gene for HPCD based on its ability to convert hpca into the yellow-colored product. This cosmid clone was further subcloned and the gene for HPCD was localized and sequenced. The open reading frame codes for a protein with 365 amino acids and M(r) = 41,699, in accord with the characteristics of the previously purified wild-type enzyme. The gene for HPCD was overexpressed in E. coli to approximately 30% of the total soluble protein, and purification of the recombinant enzyme to apparent homogeneity was achieved by a two-step procedure. Iron was the only abundant metal found in the purified recombinant enzyme, and the specific activity per iron was comparable to that observed for the wild-type enzyme. The deduced amino acid sequence of HPCD has a very high level of homology (78.6% identity in the 337-aa overlap) to the manganese-dependent homoprotocatechuate 2,3-dioxygenase (MndD) from Arthrobacter globiformis CM-2. The basis for the difference in metal selection by HPCD and MndD was investigated by mutagenesis of a 50-base-pair region of the HPCD gene containing three frame shifts relative to the MndD gene. The purified triple mutant of HPCD did not exhibit a significant change in the metal content; therefore, other factors must contribute to the selection of the active site metal.

3,4-Dihydroxyphenylacetic Acid↗
PubMed1998

Increased expression of Brevibacterium sterolicum cholesterol oxidase in Escherichia coli by genetic modification.

To improve expression of Brevibacterium sterolicum cholesterol oxidase in Escherichia coli, we utilized the T7lac promoter and modified the gene to encode the first 21 amino acids with high-expression E. coli codons. These changes resulted in a 60-fold improvement of expression level. N-terminal sequencing revealed that the E. coli produced cholesterol oxidase signal peptide is cleaved 6 amino acids closer to the N-terminus than in B. sterolicum. The recombinant E. coli produced protein is composed of 513 amino acids with a calculated Mr of 55,374. The kinetic rate constants of the recombinant protein and the B. sterolicum produced cholesterol oxidase are identical.

Amino Acid Sequence↗
PubMed1978

Stereochemical studies of hydrogen incorporation from nucleotides with fatty acid synthetase from Brevibacterium ammoniagenes.

The biosynthesis of fatty acids from malonyl-CoA and acetyl-CoA was investigated with an enzyme preparation which was purified 100-fold from Brevibacterium ammoniagenes. Fatty acids synthesized in the presence of D2O and stereospecifically deuterated NADPH and NADH were isolated and analyzed by mass chromatography to examine the localization of deuterium in the molecule. The following results were obtained: 1) HB hydrogen of NADPH was used for beta-ketoacyl reductase. 2) HB hydrogen of NADH was used for enoyl reductase. 3) Hydrogen atoms from water were found on the even-numbered methylene carbon atoms (2-hydrogen atoms per carbon atom) and some were also found on the odd-numbered methylene carbon. 4) Hydrogen atoms from NADPH were found on odd-numbered methylene carbon atoms (1-hydrogen per carbon). 5) Hydrogen atoms from NADH were also found on the odd-numbered methylene carbon atoms, but the number of incorporated hydrogen atoms was less than expected. The exchange of HB hydrogen of NADH with water catalyzed by enoyl reductase was suspected. 6) The exchange of methylene hydrogen atoms of malonyl-CoA with proton of water was suggested by 13C NMR analysis.

Brevibacterium↗
PubMed1992

Expression of Streptomyces genes encoding extracellular enzymes in Brevibacterium lactofermentum: secretion proceeds by removal of the same leader peptide as in Streptomyces lividans.

The alpha-amylase gene (amy) from Streptomyces griseus IMRU 3570 and the beta-galactosidase gene (lac) from S. lividans were subcloned into Brevibacterium lactofermentum or B. lactofermentum/Escherichia coli shuttle vectors. The amy gene was not expressed in B. lactofermentum from its own promoter but was efficiently expressed when the promoter of the kanamycin resistance gene (kan) was inserted upstream of the promoterless amylase gene. The lac gene from S. lividans was subcloned without its native promoter and was expressed when placed downstream of pBL1 promoters P2 or P3. The alpha-amylase was secreted extracellularly by removal of the same 28-amino acid leader peptide as in S. lividans. The amy and lac genes provide useful markers for selection of transformants and will facilitate the study of protein secretion in B. lactofermentum.

Amino Acid Sequence↗
PubMed1994

Construction and characterization of recA mutant strains of Corynebacterium glutamicum and Brevibacterium lactofermentum.

An internal fragment of the Corynebacterium glutamicum recA gene was amplified by the polymerase chain reaction (PCR) using degenerate primers corresponding to two short sequences that are well conserved in procaryotic RecA proteins. The deduced amino acid sequence of the amplified fragment shared significant homology with RecA sequences from other bacteria including the "invariant" and functionally conserved amino acids Leu-126, Asp-144, Gly-157, Arg-169 and Asn-193. Highest identity (91%) was shared with the gram-positive Mycobacterium tuberculosis RecA sequence. The amplified fragment was cloned into a conditional suicide vector, pBGS, and used to generate recA deficient strains of C. glutamicum and Brevibacterium lactofermentum by insertional inactivation. These strains exhibited classical RecA phenotypes including reduced recombinational activity and increased sensitivity to DNA-damaging agents such as UV irradiation, mitomycin C and methyl-methanesulphonate.

Amino Acid Sequence↗