Which enzyme is active in the absence of oxygen, such as catalase, myeloperoxidase, or lysozyme?

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From the Research

Anaerobic enzymes, such as lactate dehydrogenase (LDH) and pyruvate dehydrogenase, work in the absence of oxygen, but among the options mentioned, none are specifically anaerobic enzymes, and lysozyme breaks down bacterial cell walls regardless of oxygen presence, as supported by a study on the disruptive effect of lysozyme on the bacterial cell wall 1. Among the given options, catalase requires oxygen to function as it breaks down hydrogen peroxide into water and oxygen, and myeloperoxidase uses hydrogen peroxide to generate antimicrobial substances and also isn't anaerobic, as discussed in a study on myeloperoxidase's role in autoimmunity 2. Regarding influenza viruses,

  • genetic drift involves small, gradual mutations in viral genes that occur naturally over time, leading to minor changes in surface proteins that may reduce vaccine effectiveness,
  • genetic shift is a major, abrupt change in the influenza virus resulting from reassortment of genes between different influenza strains, potentially creating novel viruses to which humans have little immunity, which can lead to pandemics, as discussed in a study on the neuraminidase of influenza A virus 3. Drift happens continuously while shift occurs occasionally but can have more severe public health consequences. Lysozymes have been found to have various functions, including antimicrobial activity, immune-modulatory effects, and potential anti-cancer activities, as summarized in a review on the prognostic and therapeutic applications of lysozymes 4.

References

Research

The disruptive effect of lysozyme on the bacterial cell wall explored by an in-silico structural outlook.

Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology, 2018

Research

Myeloperoxidase: A new player in autoimmunity.

Cellular immunology, 2017

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