Disease relevance of amoA1

• 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 [1].
• The purification of ammonia monooxygenase from Paracoccus denitrificans [2].
• These properties indicate that this enzyme has similarities to a family of enzymes including the ammonia monooxygenase from Nitrosomonas europaea and the particulate methane monooxygenase from Methylococcus capsulatus (Bath) [2].
• Further, when expressed in the methylotroph Methylobacterium extorquens AM1, the AMO endows on this organism the ability to grow on ethene and methane [3].

High impact information on amoA1

• In cells treated this way, levels of new AMO mRNA and de novo AMO enzyme activity were correlated with increased NH4+ concentrations up to 1 mM after 3 h of incubation [4].
• Knowledge of hydroxylamine oxidoreductase, which oxidizes hydroxylamine formed by ammonia monooxygenase to nitrite, is informed by a crystal structure and detailed spectroscopic and catalytic studies [5].
• The migration of deuterium and hydrogen was observed in the aromatic hydroxylation of specifically deuterated, monosubstituted benzenes catalyzed by ammonia monooxygenase of Nitrosomonas europaea [6].
• We conclude that strongly hydrophobic amino acid sequences present in ammonia monooxygenase are responsible for the aggregation phenomenon [7].
• However, 14C-labeled forms of the membrane-bound, active-site-containing 27 kDa polypeptide of ammonia monooxygenase from Nitrosomonas europaea undergo an aggregation reaction when cells or membranes are heated in the presence of SDS-PAGE sample buffer [7].

Chemical compound and disease context of amoA1

• Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea [8].
• Inhibition of ammonia monooxygenase in Nitrosomonas europaea by carbon disulfide [9].
• Thus, the Pa. denitrificans AMO is capable of oxidizing methane to methanol, as is the case for the AMO from Nitrosomonas europaea [3].
• Kinetic characterization of the inactivation of ammonia monooxygenase in Nitrosomonas europaea by alkyne, aniline and cyclopropane derivatives [10].

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