Disease relevance of Photobacterium

• Here we report a newly determined crystal structure of the dimeric Cu,Zn superoxide dismutase from Photobacterium leiognathi (crystallized in space group R32, refined at 2.5 A resolution, R-factor 0.19) and analyse it in comparison with that of the monomeric enzyme from Escherichia coli [1].
• Fluorescence dynamics measurements have been made on the bioluminescence reaction intermediates using Photobacterium leiognathi, Vibrio fischeri, and Vibrio harveyi luciferases, both alone and in mixtures with Photobacterium phosphoreum lumazine protein [2].
• The resonance coherent anti-Stokes Raman technique was used to obtain vibrational spectra of flavin in flavodoxins from Desulfovibrio gigas and Desulfovibrio vulgaris and of the simpler 6,7-dimethyl-8-ribityllumazine chromophore in the blue fluorescence lumazine protein from the bioluminescent bacterium Photobacterium phosphoreum [3].
• The flo gene, which confers resistance to florfenicol and chloramphenicol, has previously been identified in Photobacterium piscicida and Salmonella enterica serovar Typhimurium DT104 [4].
• Nine chemically defined inoculation diluents, with compositions ranging from 0.85% NaCl to 35% marine salts, were used to evaluate the influence of diluent composition on the biochemical profiles of 30 marine and estuarine bacterial strains, including species of Vibrio, Aeromonas, Allomonas, and Photobacterium [5].

High impact information on Photobacterium

• A library of Photobacterium phosphoreum DNA was screened in lambda 2001 for the lumazine protein gene, using two degenerate 17-mer oligonucleotide probes that were deduced from a partial protein primary sequence [6].
• The presence of a copper/zinc superoxide dismutase in the bacterium Photobacterium leiognathi: a likely case of gene transfer from eukaryotes to prokaryotes [7].
• Cloning and expression of the Photobacterium phosphoreum luminescence system demonstrates a unique lux gene organization [8].
• Bacteriocuprein superoxide dismutase of Photobacterium leiognathi. Isolation and sequence of the gene and evidence for a precursor form [9].
• Fatty acid reduction in Photobacterium phosphoreum is catalyzed in a coupled reaction by two enzymes: acyl-protein synthetase, which activates fatty acids (+ATP), and a reductase, which reduces activated fatty acids (+NADPH) to aldehyde [10].

Chemical compound and disease context of Photobacterium

• The luminescent bacterium Photobacterium phosphoreum has been shown to possess a fatty acid reductase based on the stimulation of the aldehyde-dependent luminescent reaction on incubation of the enzyme with ATP, NADPH, and tetradecanoic acid (Riendeau, D., and Meighen, E. (1979) J. Biol. Chem. 254, 7488-7490) [11].
• The enzyme responsible for the stimulation by ATP AND NADPH of light emission catalyzed by bacterial luciferase has been partially purified from extracts of the luminescent bacterium, Photobacterium phosphoreum [12].
• Lumazine protein, a novel protein containing 6,7-dimethyl-8-ribityllumazine as a bound prosthetic group, is one of the several major proteins produced by the bioluminescent bacteria, Photobacterium phosphoreum. purification to complete homogeneity from cell extracts is achieved in six steps [13].
• Differential acylation in vitro with tetradecanoyl coenzyme A and tetradecanoic acid (+ATP) of three polypeptides shown to have induced synthesis in Photobacterium phosphoreum [14].
• Crystals of a copper-zinc superoxide dismutase from Photobacterium leiognathi, a luminescent marine bacterium that is the species-specific symbiont of the ponyfish, have been obtained from 2-methyl-2,4-pentanediol solutions [15].

Biological context of Photobacterium

• Therefore, protection of Escherichia coli mutants deficient in SOD and DNA repair genes (sod-, xth-, and nfo-) was demonstrated by transforming the mutant strain with a plasmid pYK9 that encoded Photobacterium leiognathi CuZnSOD and human AP endonuclease [16].
• The lumazine protein-encoding gene in Photobacterium leiognathi is linked to the lux operon [17].
• Nucleotide sequence of the luxG gene (GenBank Accession No. AF053227) from Photobacterium leiognathi PL741 has been determined, and the encoded probable flavin reductase is deduced [18].
• Comparison of the amino acid sequence of swordfish liver copper/zinc superoxide dismutase with the bovine, human, horse, yeast and Photobacterium leiognathi indicates that the swordfish enzyme has a high homology with the other eukaryotic enzymes [19].
• Covalent reaction of cerulenin at the active site of acyl-CoA reductase of Photobacterium phosphoreum [20].

Gene context of Photobacterium

• An rpoE-like locus controls outer membrane protein synthesis and growth at cold temperatures and high pressures in the deep-sea bacterium Photobacterium sp. strain SS9 [21].
• To more fully explore the role of unsaturated fatty acids in high-pressure, low-temperature growth, the fabF gene from the psychrotolerant, piezophilic deep-sea bacterium Photobacterium profundum strain SS9 was characterized and its role and regulation were examined [22].
• Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex [23].
• Cu,Zn superoxide dismutase from Photobacterium leiognathi has been cloned and expressed in Escherichia coli [24].
• In contrast, the Photobacterium fischeri NAD(P)H-FMN oxidoreductase FRG showed the same ping-pong mechanism in both the single-enzyme spectrophotometric and the luciferase-coupled assays [25].

Analytical, diagnostic and therapeutic context of Photobacterium

• The catalytic activity of a mutant of Photobacterium leiognathi Cu, Zn superoxide dismutase in which the Glu59 residue, conserved in most bacterial variants of the enzyme, has been replaced by glutamine was investigated by pulse radiolysis [26].

References