Abstract
Functional analyses of peroxidases are a major challenge. In silico analysis appears to be a powerful tool to overcome at least some of the problems that arose from (1) the numerous possible functions of peroxidases, (2) their low substrate specificity, and (3) the compensation of knockout mutants by other isoenzymes. Amino acid sequences and crystal structures of peroxidases were used for the prediction of tertiary structures, posttranslational modifications, ligand and substrate binding sites, and so on of uncharacterized peroxidases. This protocol presents tools and their applications for an in silico analysis of soluble and membrane-bound peroxidases, but it may be used for other proteins, too.
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Acknowledgments
This work was supported by a PhD student grant to K. R. from the Dr. Elisabeth Appuhn Foundation.
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Lüthje, S., Ramanathan, K. (2020). In Silico Analysis of Class III Peroxidases: Hypothetical Structure, Ligand Binding Sites, Posttranslational Modifications, and Interaction with Substrates. In: Jorrin-Novo, J., Valledor, L., Castillejo, M., Rey, MD. (eds) Plant Proteomics. Methods in Molecular Biology, vol 2139. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0528-8_24
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DOI: https://doi.org/10.1007/978-1-0716-0528-8_24
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