Abstract
Catalase plays a central role in plant stress responses but is highly susceptible to photoinhibition. A rice catalase-B protein avoiding photoinhibition was developed by mutagenesis of specific amino acids: Leu-189 to Trp-189 and His-225 to Thr-225 and then recombinantly expressed in E. coli. In addition, the site specific mutation also induced 2–2.5-fold increase in enzyme velocity with high affinity for its substrate and showed nearly a 3-fold lower K m than the wild protein. These characteristic of mutated rice catalase-B is highly promising in transgenic research to increase plant productivity under stress conditions.
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The authors are thankful to The Director, Institute of Life Sciences, Orissa, for support. MR gratefully acknowledges the UGC for financial help.
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Mondal, P., Ray, M., Kar, M. et al. Molecular identification and properties of a light-insensitive rice catalase-B expressed in E. coli . Biotechnol Lett 30, 563–568 (2008). https://doi.org/10.1007/s10529-007-9553-9
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DOI: https://doi.org/10.1007/s10529-007-9553-9