What question did this study set out to answer?

To investigate how mutations can enhance the catalytic activity of RuBisCo in thermococcus kodakarensis.

April 29, 2026Journal of Agricultural and Food Chemistry0 citations

Enhancing the Catalytic Activity of Thermococcus kodakarensis RuBisCo via Computer-Aided Rational Design

SLSainan LiBroad Institute JZJin ZhouChongqing University of Posts and Telecommunications XSXiangfei SongEnergy Institute

Key Points

To investigate how mutations can enhance the catalytic activity of RuBisCo in thermococcus kodakarensis.
Analyzed Y168L-A361P mutation effects using H NMR results
Conducted molecular-dynamics simulations to assess binding interactions
Y168L-A361P mutation significantly increases carboxylation rate compared to oxygenation rate
Molecular simulations show enhanced binding through a robust hydrogen bond network

Abstract

H NMR results demonstrated that the Y168L-A361P mutation enhances the carboxylation rate to a much greater extent than does the oxygenation rate. Molecular-dynamics simulations revealed that Y168L and A361P─although neither contacts the substrate directly─augment binding of the carboxylation intermediate EI II through an extended interaction network that strengthens hydrogen bonds to the substrate carboxylate.

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