Disease relevance of Brevibacterium

• The gene coding for a CGCG specific DNA methylase has been cloned in E. coli from Brevibacterium epidermidis [1].
• Resonance Raman spectra of Rhodococcus sp. R312 (formerly Brevibacterium sp. R312) nitrile hydratase, a novel non-heme iron enzyme, have a large number of peaks in the 300-500 cm-1 region; observation of shifts in these peaks after labeling with 34S shows that they arise from cysteine coordinated to the ferric ion in the protein [2].
• In brush borders treated with Brevibacterium sp. or Nocardia erythropolis cholesterol oxidases, a significant fraction of the free cholesterol was oxidized rapidly, without glutaraldehyde fixation, and the remaining cholesterol was oxidized at a slower rate [3].
• Corynebacterium (Brevibacterium), which is well known in the production of L-glutamic acid, was selected as a starting strain for the breeding of an L-arginine producer and has been used on a commercial scale [4].
• Its protein product, ChoE, is homologous to other secreted cholesterol oxidases identified in Brevibacterium sterolicum and Streptomyces spp [5].

High impact information on Brevibacterium

• Wild-type Brevibacterium flavum has been shown to possess arogenate dehydrogenase activity and to lack prephenate dehydrogenase, thereby providing presumptive evidence that arogenate (previously named "pretyrosine") is an obligatory intermediate of L-tyrosine biosynthesis [6].
• A multienzyme fatty acid synthetase complex isolated from Brevibacterium ammoniagenes has been purified to a specific activity of 1440 nmol of malonyl-CoA incorporated per min/mg [7].
• Cholesterol oxidase from Brevibacterium sterolicum is a monomeric flavoenzyme catalyzing the oxidation and isomerization of cholesterol to cholest-4-en-3-one [8].
• Brevibacterium sterolicum possesses two forms of cholesterol oxidase, one containing noncovalently bound FAD, the second containing a FAD covalently linked to His(69) of the protein backbone [9].
• Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity [10].

Chemical compound and disease context of Brevibacterium

• Glutamic acid producer Brevibacterium lactofermentum intact cells were used to demonstrate the feasibility of in vivo 15N NMR to follow nitrogen assimilation and amino acid production throughout the growth cycle [11].
• A protocatechuate 3,4-dioxygenase with exceptionally sharp spectral features and a new subunit composition has been purified and crystallized from the Gram-positive organism Brevibacterium fuscum [12].
• Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes [13].
• Mechanism of the adenylate cyclase reaction. Stereochemistry of the reaction catalyzed by the enzyme from Brevibacterium liquefaciens [14].
• Adenylate cyclase from Brevibacterium liquefaciens (ATCC 14929) catalyzes the formation of the RP-diastereomer of adenosine 3':5'-cyclic monophosphorothioate from the SP-diastereomer of adenosine-5'-(1-thiotriphosphate) [14].

Biological context of Brevibacterium

• The binding reactions of two heterocyclic analogs of protocatechuate (PCA), 2-hydroxyisonicotinic acid N-oxide and 6-hydroxynicotinic acid N-oxide, to Brevibacterium fuscum protocatechuate 3,4-dioxygenase have been characterized [15].
• Nucleotide sequence of the homoserine kinase (thr B) gene of Brevibacterium lactofermentum [16].
• Fe K-edge EXAFS studies of the spectroscopically similar protocatechuate 3,4-dioxygenase from Brevibacterium fuscum are consistent with a pentacoordinate geometry of the iron active site with 3 O/N ligands at 1.90 A and 2 O/N ligands at 2.08 A [17].
• The spectinomycin and streptomycin resistance plasmid pCG4, originally from Corynebacterium glutamicum T250, could transform various glutamate-producing bacteria such as C. glutamicum, Corynebacterium herculis, Brevibacterium flavum, and Microbacterium ammoniaphilum [18].
• The Brevibacterium acetylicum gsk gene, which encodes guanosine kinase (ATP:guanosine 5'-phosphotransferase), a kinase that is involved in guanosine salvage pathways, has been cloned by using the N-terminal amino acid sequence of the purified protein [19].

Anatomical context of Brevibacterium

• Degradative and n.m.r.-spectroscopic studies have been carried out on a novel mannitol teichoic acid extracted from the cell wall of bacterium N.C.T.C. 9742, for which the name Brevibacterium iodinum has been proposed [20].
• The effects of Brevibacterium sp. cholesterol oxidase on the cholesterol content of LLC-PK1 cells, an epithelial cell line with multiple differentiated characteristics of the renal proximal tubule, were investigated [21].
• Commercial cholesterol esterase from bovine pancreas and cholesterol oxidase from Brevibacterium recombinant type have been immobilized individually and co-immobilized on to arylamine glass beads (pore diameter, 55 nm) through diazotization [22].
• For cells of Brevibacterium sp. under conditions of biotin limitation, the efflux of metabolites through the cell membrane was affected by temperature [23].
• A positive genetic transfer by protoplast fusion was obtained in auxotrophic mutants Brevibacterium sp. M27 his and Brevibacterium sp. M27 arg [24].

Gene context of Brevibacterium

• The Brevibacterium lactofermentum argS gene, which encodes an arginyl-tRNA synthetase, was identified in the upstream region of the lysA gene [25].
• Identification, characterization, and chromosomal organization of the ftsZ gene from Brevibacterium lactofermentum [26].
• Five DNA fragments carrying the thrB gene (homoserine kinase E.C. 2.7.1.39) of Brevibacterium lactofermentum were cloned by complementation of Escherichia coli thrB mutants using pBR322 as vector [27].
• The highest identity values were found for ORF1 with the theta replicase (acc. no. U39878) of Brevibacterium linens (58.8%) and ORF6 with the recombinase/invertase (acc. no. AF060871) found in Rhodococcus rhodochrous (46.4%) [28].
• The Brevibacterium albidum gene encoding the arginine tRNACCG complements the growth defect of an Escherichia coli strain carrying a thermosensitive mutation in the rnpA gene at the nonpermissive temperature [29].

Analytical, diagnostic and therapeutic context of Brevibacterium

• Brevibacterium fuscum protocatechuate 3,4-dioxygenase. Purification, crystallization, and characterization [12].
• Cloning and sequence determination of the aspartase-encoding gene from Brevibacterium flavum MJ233 [30].
• Simultaneous identification of two cyclohexanone oxidation genes from an environmental Brevibacterium isolate using mRNA differential display [31].
• Molecular cloning and transcriptional analysis of a guanosine kinase gene of Brevibacterium acetylicum ATCC 953 [19].
• Site-directed mutagenesis of the aspartokinase gene lysC and its characterization in Brevibacterium flavum [32].

References