Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related

Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related

Received 19 July 1995; revised 16 August 1995; accepted 16 August 1995 | Andrew J. Holmes, Andria Costello, Mary E. Lidstrom, J. Colin Murrell
The study by Holmes et al. (1995) investigates the evolutionary relationship between particulate methane monooxygenase (pMMO) and ammonia monooxygenase (AMO) enzymes, which are crucial for methane and ammonia oxidation, respectively. The researchers designed degenerate primers based on shared amino acid sequences between the 27-kDa polypeptides of pMMO and AMO. These primers were used to amplify and sequence the *pmoA* and *amoA* genes from a diverse range of methanotrophic and nitrifying bacteria. The results showed high sequence identity and conservation in both primary and secondary structures of the predicted amino acid sequences. Notably, *Nitrosococcus oceanus* AMO showed higher identity to *γ-Proteobacteria* pMMO sequences than to *β-Proteobacteria* AMO sequences. This suggests that pMMO and AMO are evolutionarily related enzymes despite their different physiological roles. The study also highlights the potential significance of these enzymes in bioremediation and the importance of further research to understand their biochemistry and applications.The study by Holmes et al. (1995) investigates the evolutionary relationship between particulate methane monooxygenase (pMMO) and ammonia monooxygenase (AMO) enzymes, which are crucial for methane and ammonia oxidation, respectively. The researchers designed degenerate primers based on shared amino acid sequences between the 27-kDa polypeptides of pMMO and AMO. These primers were used to amplify and sequence the *pmoA* and *amoA* genes from a diverse range of methanotrophic and nitrifying bacteria. The results showed high sequence identity and conservation in both primary and secondary structures of the predicted amino acid sequences. Notably, *Nitrosococcus oceanus* AMO showed higher identity to *γ-Proteobacteria* pMMO sequences than to *β-Proteobacteria* AMO sequences. This suggests that pMMO and AMO are evolutionarily related enzymes despite their different physiological roles. The study also highlights the potential significance of these enzymes in bioremediation and the importance of further research to understand their biochemistry and applications.
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