Disease relevance of Chromobacterium

• Cloning and expression of Chromobacterium violaceum phenylalanine hydroxylase in Escherichia coli and comparison of amino acid sequence with mammalian aromatic amino acid hydroxylases [1].
• Using mice deficient in generating phagocyte superoxide (p47(phox)(-/-)) and mice deficient in generating inducible nitric oxide synthase (iNOS(-/-)), we examined the roles of these reactive species in host defense against Burkholderia cepacia and Chromobacterium violaceum, organisms known to have unusual virulence in chronic granulomatous disease [2].
• We evaluated four acyl-HSL bioreporters, based on tra of Agrobacterium tumefaciens, lux of Vibrio fischeri, las of Pseudomonas aeruginosa, and pigment production by Chromobacterium violaceum, for their ability to detect sets of 3-oxo acyl-HSLs, 3-hydroxy acyl-HSLs, and alkanoyl-HSLs with chain lengths ranging from C4 to C12 [3].
• Freshwater isolates of Janthinobacterium lividum and Chromobacterium violaceum produced the purple pigment violacein and exhibited acute toxicity to the nanoflagellates tested [4].
• Glucose-6-phosphate dehydrogenase deficiency, neutrophil dysfunction and Chromobacterium violaceum sepsis [5].

High impact information on Chromobacterium

• Violacein, a pigment isolated from Chromobacterium violaceum in the Amazon River, presents diverse biologic properties and attracts interest as a consequence of its antileukemic activity [6].
• Phenylalanine hydroxylase from Chromobacterium violaceum. Uncoupled oxidation of tetrahydropterin and the role of iron in hyroxylation [7].
• L-tryptophan 2',3'-oxidase from Chromobacterium violaceum. Substrate specificity and mechanistic implications [8].
• Phenylalanine hydroxylase from Chromobacterium violaceum. Purification and characterization [9].
• Tetrameric full-length human PAH, dimeric double-truncated (DeltaN102-DeltaC428) human PAH, and monomeric Chromobacterium violaceum PAH were PEGylated with succinimidyl succinate polyethylene glycol of molecular weight 5000 or 20,000 Da [10].

Chemical compound and disease context of Chromobacterium

• Purification and partial characterization of an amino acid alpha,beta- dehydrogenase, L-tryptophan 2',3'-oxidase from Chromobacterium violaceum [11].
• FK228 (formerly FR901228) was recently isolated from Chromobacterium violaceum as a potent antitumor agent and its biologic target protein was identified as histone deacetylase (HDAC) [12].
• Steady-state kinetic analysis of pterin-dependent phenylalanine hydroxylase from Chromobacterium violaceum indicated that the enzyme follows a partially ordered reaction mechanism [13].
• Identification of metal ligands in Cu(II)-inhibited Chromobacterium violaceum phenylalanine hydroxylase by electron spin echo envelope modulation analysis of histidine to serine mutations [14].
• The Chromobacterium violaceum activity assay illustrates that reactions between 3-oxo acylated homoserine lactone molecules and oxidized halogens do occur despite the presence of biofilm components at much greater concentrations [15].

Biological context of Chromobacterium

• Phenylalanine hydroxylase from Chromobacterium violaceum is a copper-containing monooxygenase. Kinetics of the reductive activation of the enzyme [16].
• SWI inhibited violacein production, a phenotype that is regulated by quorum sensing in Chromobacterium violaceum [17].
• According to recent crystallographic studies, residue Tyr179 in Chromobacterium violaceum phenylalanine hydroxylase is located in the active site and its hydroxyl oxygen is 5.1 A from the iron, where it has been suggested to play a role in positioning the pterin cofactor [18].
• AIMS: The biotransformation study of the pigment (violacein) produced by Chromobacterium violaceum, was verified by its decolorization utilizing six different organisms in liquid and solid media [19].
• Intraspecies variation of Chromobacterium violaceum was examined by comparative sequence - and by restriction fragment length polymorphism analysis of the recombinase A gene (recA-PCR-RFLP) [20].

Anatomical context of Chromobacterium

• Arphamenine A was synthesized in a cell-free system obtained from the arphamenine-producing strain, Chromobacterium violaceum BMG361-CF4 [21].

Gene context of Chromobacterium

• It is thus of interest to compare the structure of the divergent Chromobacterium violaceum phenylalanine hydroxylase (CvPheOH) ( approximately 24% sequence identity overall) to the related human and rat PheOH structures [22].
• Cloning, molecular analysis, and expression of the polyhydroxyalkanoic acid synthase (phaC) gene from Chromobacterium violaceum [23].
• Genotyping of Chromobacterium violaceum isolates by recA PCR-RFLP analysis [20].
• Action of FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum no. 968, on Ha-ras transformed NIH3T3 cells [24].
• beta-Lactamase activity in Chromobacterium violaceum [25].

Analytical, diagnostic and therapeutic context of Chromobacterium

• The Chromobacterium violaceum CV026 bioassay was used to determine the effects of such reactions on acylated homoserine lactone activity [15].
• Sequence analysis and functional characterization of the violacein biosynthetic pathway from Chromobacterium violaceum [26].

References