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Gene Review

amoA1  -  ammonia monooxygenase

Nitrosomonas europaea ATCC 19718

 
 
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Disease relevance of amoA1

 

High impact information on amoA1

 

Chemical compound and disease context of amoA1

 

Biological context of amoA1

  • Native marine bacteria containing amoA could also be detected at their naturally occurring titer in oligotrophic seawater [11].
  • Nitrosomonas europaea, a chemolithotrophic bacterium, was found to contain two copies of the gene coding for the presumed active site polypeptide of ammonia monooxygenase, the 32-kDa acetylene-binding polypeptide [12].
  • Immediately downstream of this gene, in the same operon, is the gene for a 40-kDa polypeptide that copurifies with the ammonia monooxygenase acetylene-binding polypeptide [12].
  • Ammonia oxidizer diversity within each grassland soil was assessed by PCR amplification of microbial community DNA with both ammonia oxidizer-specific, 16S rRNA gene (rDNA) and functional, amoA, gene primers [13].
  • The nucleotide sequences of the two copies of amoA were obtained, and they were found to differ by one nucleotide [14].
 

Associations of amoA1 with chemical compounds

  • To correlate new levels of mRNA with de novo activity, existent mRNA pools and AMO activity were depleted prior to induction by NH4+ [4].
  • It is proposed that CS2 may act on AMO by reversibly reacting with a suitable nucleophilic amino acid in close proximity to the active site copper [9].
  • Measurements of ammonia-dependent O2 consumption, which depends on AMO, confirmed that the slower-growing mutant had lower activity while the faster-growing mutant had near wild-type levels of activity [14].
  • We demonstrate that methyl fluoride and dimethyl ether are substrates for ammonia monooxygenase and are converted to formaldehyde and a mixture of methanol and formaldehyde, respectively [8].
  • Inhibition of membrane-bound methane monooxygenase and ammonia monooxygenase by diphenyliodonium: implications for electron transfer [15].
 

Analytical, diagnostic and therapeutic context of amoA1

  • PCR products were analysed by denaturing gradient gel electrophoresis, phylogenetic analysis of partial 16S rDNA and amoA sequences, and hybridization with ammonia oxidizer-specific oligonucleotide probes [13].
  • Northern blot analysis of transcription likewise showed that the slower-growing mutant had less full-sized AMO mRNA [14].
  • However, comparative sequence analysis of 13 amoA clone sequences from activated sludge demonstrated that these sequences were highly similar to each other and to the corresponding amoA gene fragments of Nitrosomonas europaea Nm50 and the N. mobilis isolate [16].
  • The genetic diversity and expression of amoA of autotrophic ammonia oxidizers in wastewater treatment processes were investigated by RT-PCR and denaturing gradient gel electrophoresis (DGGE) in order to identify active components of ammonia-oxidizer populations in a such processes [17].

References

  1. 14C2H2- and 14CO2-labeling studies of the de novo synthesis of polypeptides by Nitrosomonas europaea during recovery from acetylene and light inactivation of ammonia monooxygenase. Hyman, M.R., Arp, D.J. J. Biol. Chem. (1992) [Pubmed]
  2. The purification of ammonia monooxygenase from Paracoccus denitrificans. Moir, J.W., Crossman, L.C., Spiro, S., Richardson, D.J. FEBS Lett. (1996) [Pubmed]
  3. Heterologous expression of heterotrophic nitrification genes. Crossman, L.C., Moir, J.W., Enticknap, J.J., Richardson, D.J., Spiro, S. Microbiology (Reading, Engl.) (1997) [Pubmed]
  4. Induction of ammonia monooxygenase and hydroxylamine oxidoreductase mRNAs by ammonium in Nitrosomonas europaea. Sayavedra-Soto, L.A., Hommes, N.G., Russell, S.A., Arp, D.J. Mol. Microbiol. (1996) [Pubmed]
  5. Metabolism of inorganic N compounds by ammonia-oxidizing bacteria. Arp, D.J., Stein, L.Y. Crit. Rev. Biochem. Mol. Biol. (2003) [Pubmed]
  6. NIH shift in the hydroxylation of aromatic compounds by the ammonia-oxidizing bacterium Nitrosomonas europaea. Evidence against an arene oxide intermediate. Vannelli, T., Hooper, A.B. Biochemistry (1995) [Pubmed]
  7. An electrophoretic study of the thermal- and reductant-dependent aggregation of the 27 kDa component of ammonia monooxygenase from Nitrosomonas europaea. Hyman, M.R., Arp, D.J. Electrophoresis (1993) [Pubmed]
  8. Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea. Hyman, M.R., Page, C.L., Arp, D.J. Appl. Environ. Microbiol. (1994) [Pubmed]
  9. Inhibition of ammonia monooxygenase in Nitrosomonas europaea by carbon disulfide. Hyman, M.R., Kim, C.Y., Arp, D.J. J. Bacteriol. (1990) [Pubmed]
  10. Kinetic characterization of the inactivation of ammonia monooxygenase in Nitrosomonas europaea by alkyne, aniline and cyclopropane derivatives. Keener, W.K., Russell, S.A., Arp, D.J. Biochim. Biophys. Acta (1998) [Pubmed]
  11. Amplification of the amoA gene from diverse species of ammonium-oxidizing bacteria and from an indigenous bacterial population from seawater. Sinigalliano, C.D., Kuhn, D.N., Jones, R.D. Appl. Environ. Microbiol. (1995) [Pubmed]
  12. Sequence of the gene coding for ammonia monooxygenase in Nitrosomonas europaea. McTavish, H., Fuchs, J.A., Hooper, A.B. J. Bacteriol. (1993) [Pubmed]
  13. Grassland management regimens reduce small-scale heterogeneity and species diversity of beta-proteobacterial ammonia pxidizer populations. Webster, G., Embley, T.M., Prosser, J.I. Appl. Environ. Microbiol. (2002) [Pubmed]
  14. Mutagenesis and expression of amo, which codes for ammonia monooxygenase in Nitrosomonas europaea. Hommes, N.G., Sayavedra-Soto, L.A., Arp, D.J. J. Bacteriol. (1998) [Pubmed]
  15. Inhibition of membrane-bound methane monooxygenase and ammonia monooxygenase by diphenyliodonium: implications for electron transfer. Shiemke, A.K., Arp, D.J., Sayavedra-Soto, L.A. J. Bacteriol. (2004) [Pubmed]
  16. Combined molecular and conventional analyses of nitrifying bacterium diversity in activated sludge: Nitrosococcus mobilis and Nitrospira-like bacteria as dominant populations. Juretschko, S., Timmermann, G., Schmid, M., Schleifer, K.H., Pommerening-Röser, A., Koops, H.P., Wagner, M. Appl. Environ. Microbiol. (1998) [Pubmed]
  17. Comparative analysis of genetic diversity and expression of amoA in wastewater treatment processes. Ebie, Y., Noda, N., Miura, H., Matsumura, M., Tsuneda, S., Hirata, A., Inamori, Y. Appl. Microbiol. Biotechnol. (2004) [Pubmed]
 
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