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MeSH Review

Chloroflexus

 
 
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Disease relevance of Chloroflexus

 

High impact information on Chloroflexus

  • Propionyl-coenzyme A synthase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO2 fixation [4].
  • A bicyclic autotrophic CO2 fixation pathway in Chloroflexus aurantiacus [1].
  • The stability of tetrameric malate dehydrogenase from the green phototrophic bacterium Chloroflexus aurantiacus (CaMDH) is at least in part determined by electrostatic interactions at the dimer-dimer interface [5].
  • Malate dehydrogenase (MDH) from the moderately thermophilic bacterium Chloroflexus aurantiacus (CaMDH) is a tetrameric enzyme, while MDHs from mesophilic organisms usually are dimers [6].
  • The biochemical and biophysical data obtained for arsenite oxidase in the green filamentous bacterium Chloroflexus aurantiacus allow a structural model of the enzyme's membrane association to be proposed [7].
 

Chemical compound and disease context of Chloroflexus

  • Functioning of quinone acceptors in the reaction center of the green photosynthetic bacterium Chloroflexus aurantiacus [8].
  • Photosynthetic sulfide oxidation by Chloroflexus aurantiacus, a filamentous, photosynthetic, gliding bacterium [9].
  • Two strains of the gliding phototrophic bacterium Chloroflexus aurantiacus were investigated for the presence of lipopolysaccharide (LPS) [10].
  • Bacteriochlorophyll c formation via the C5 pathway of 5-aminolevulinic acid synthesis in Chloroflexus aurantiacus [11].
  • Biosynthesis of 5-aminolevulinic acid (ALA) in Chloroflexus aurantiacus, a thermophilic bacterium forming bacteriochlorophyll c, is shown to proceed via the C5 pathway by demonstrating (1) the specific labeling of its chlorin ring with [1 - 13C]glutamate and (2) the enzyme activity to produce ALA from glutamate in a cell-free extract [11].
 

Anatomical context of Chloroflexus

 

Gene context of Chloroflexus

  • Both are unique among the 16S rRNA sequences of cultivated members of this group, including an Octopus Spring isolate of Chloroflexus aurantiacus and Heliothrix oregonensis, whose sequences we report herein [12].
  • Subunit structure of ATP synthase from Chloroflexus aurantiacus [13].
  • The gene encoding malate dehydrogenase (MDH) from Chloroflexus aurantiacus was cloned, sequenced, and analyzed [14].
  • Autotrophically grown Chloroflexus cells contained acetyl-CoA carboxylase and propionyl-CoA carboxylase activity [15].
  • All-cis hentriaconta-9,15,22-triene (I) has been isolated from Chloroflexus mats, Yellowstone National Park (USA), and identified by GC-(HR)MS analysis of I and its hydrogenated and DMDS-derivatized products and by 1H and 13C NMR spectroscopy [16].

References

  1. A bicyclic autotrophic CO2 fixation pathway in Chloroflexus aurantiacus. Herter, S., Fuchs, G., Bacher, A., Eisenreich, W. J. Biol. Chem. (2002) [Pubmed]
  2. A comparative study of bchG from green photosynthetic bacteria. Garcia-Gil, L.J., Gich, F.B., Fuentes-Garcia, X. Arch. Microbiol. (2003) [Pubmed]
  3. Lipid biomarkers for bacterial ecosystems: studies of cultured organisms, hydrothermal environments and ancient sediments. Summons, R.E., Jahnke, L.L., Simoneit, B.R. Ciba Found. Symp. (1996) [Pubmed]
  4. Propionyl-coenzyme A synthase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO2 fixation. Alber, B.E., Fuchs, G. J. Biol. Chem. (2002) [Pubmed]
  5. Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface. Bjørk, A., Dalhus, B., Mantzilas, D., Sirevåg, R., Eijsink, V.G. J. Mol. Biol. (2004) [Pubmed]
  6. Stabilization of a tetrameric malate dehydrogenase by introduction of a disulfide bridge at the dimer-dimer interface. Bjørk, A., Dalhus, B., Mantzilas, D., Eijsink, V.G., Sirevåg, R. J. Mol. Biol. (2003) [Pubmed]
  7. Arsenite oxidase, an ancient bioenergetic enzyme. Lebrun, E., Brugna, M., Baymann, F., Muller, D., Lièvremont, D., Lett, M.C., Nitschke, W. Mol. Biol. Evol. (2003) [Pubmed]
  8. Functioning of quinone acceptors in the reaction center of the green photosynthetic bacterium Chloroflexus aurantiacus. Kutuzov, M.A., Mamedov, M.D., Semenov AYu, n.u.l.l., Shinkarev, V.P., Verkhovsky, M.I., Abdulaev, N.G., Drachev, L.A. FEBS Lett. (1991) [Pubmed]
  9. Photosynthetic sulfide oxidation by Chloroflexus aurantiacus, a filamentous, photosynthetic, gliding bacterium. Madigan, M.T., Brock, T.D. J. Bacteriol. (1975) [Pubmed]
  10. Absence of a characteristic cell wall lipopolysaccharide in the phototrophic bacterium Chloroflexus aurantiacus. Meissner, J., Krauss, J.H., Jürgens, U.J., Weckesser, J. J. Bacteriol. (1988) [Pubmed]
  11. Bacteriochlorophyll c formation via the C5 pathway of 5-aminolevulinic acid synthesis in Chloroflexus aurantiacus. Oh-hama, T., Santander, P.J., Stolowich, N.J., Scott, A.I. FEBS Lett. (1991) [Pubmed]
  12. Uncultivated cyanobacteria, Chloroflexus-like inhabitants, and spirochete-like inhabitants of a hot spring microbial mat. Weller, R., Bateson, M.M., Heimbuch, B.K., Kopczynski, E.D., Ward, D.M. Appl. Environ. Microbiol. (1992) [Pubmed]
  13. Subunit structure of ATP synthase from Chloroflexus aurantiacus. Yanyushin, M.F. FEBS Lett. (1993) [Pubmed]
  14. Malate dehydrogenase from the green gliding bacterium Chloroflexus aurantiacus is phylogenetically related to lactic dehydrogenases. Synstad, B., Emmerhoff, O., Sirevåg, R. Arch. Microbiol. (1996) [Pubmed]
  15. 13C-NMR study of autotrophic CO2 fixation pathways in the sulfur-reducing Archaebacterium Thermoproteus neutrophilus and in the phototrophic Eubacterium Chloroflexus aurantiacus. Strauss, G., Eisenreich, W., Bacher, A., Fuchs, G. Eur. J. Biochem. (1992) [Pubmed]
  16. All-cis hentriaconta-9,15,22-triene in microbial mats formed by the phototrophic prokaryote Chloroflexus. van der Meer, M.T., Schouten, S., Ward, D.M., Geenevasen, J.A., Sinninghe Damste, J.S. Org. Geochem. (1999) [Pubmed]
 
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