The Structural Biology of Catalase Evolution
- PMID: 38963482
- DOI: 10.1007/978-3-031-58843-3_3
The Structural Biology of Catalase Evolution
Abstract
Catalases are essential enzymes for removal of hydrogen peroxide, enabling aerobic and anaerobic metabolism in an oxygenated atmosphere. Monofunctional heme catalases, catalase-peroxidases, and manganese catalases, evolved independently more than two billion years ago, constituting a classic example of convergent evolution. Herein, the diversity of catalase sequences is analyzed through sequence similarity networks, providing the context for sequence distribution of major catalase families, and showing that many divergent catalase families remain to be experimentally studied.
Keywords: Catalase; Enzyme evolution; Hydrogen peroxide; Sequence similarity networks.
© 2024. The Author(s), under exclusive license to Springer Nature Switzerland AG.
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References
-
- Alfonso-Prieto M, Biarnés X, Vidossich P, Rovira C (2009) The molecular mechanism of the catalase reaction. J Am Chem Soc 131:11751–11761. https://doi.org/10.1021/ja9018572 - DOI - PubMed
-
- Alfonso-Prieto M, Vidossich P, Rovira C (2012) The reaction mechanisms of heme catalases: an atomistic view by ab initio molecular dynamics. Arch Biochem Biophys 525:121–130. https://doi.org/10.1016/j.abb.2012.04.004 - DOI - PubMed
-
- Atkinson HJ, Babbitt PC (2009) An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations. PLoS Comput Biol 5:e1000541. https://doi.org/10.1371/journal.pcbi.1000541 - DOI - PubMed - PMC
-
- Atkinson HJ, Morris JH, Ferrin TE, Babbitt PC (2009) Using sequence similarity networks for visualization of relationships across diverse protein Superfamilies. PLoS One 4:e4345. https://doi.org/10.1371/journal.pone.0004345 - DOI - PubMed - PMC
-
- Baier F, Tokuriki N (2014) Connectivity between catalytic landscapes of the metallo-β-lactamase superfamily. J Mol Biol 426:2442–2456. https://doi.org/10.1016/j.jmb.2014.04.013 - DOI - PubMed
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