Article
Mutation design of a thermophilic Rubisco based on three-dimensional structure enhances its activity at ambient temperature.
Proteins - 1 Oct 2016
Fujihashi Masahiro, Nishitani Yuichi, Kiriyama Tomohiro, Aono Riku, Sato Takaaki, Takai Tomoyuki, Tagashira Kenta, Fukuda Wakao, Atomi Haruyuki, Imanaka Tadayuki, Miki Kunio
Abstract excerpt
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) plays a central role in carbon dioxide fixation on our planet. Rubisco from a hyperthermophilic archaeon Thermococcus kodakarensis (Tk-Rubisco) shows approximately twenty times the activity of spinach Rubisco at high temperature, but only one-eighth the activity at ambient temperature. We have tried to improve the activity of Tk-Rubisco at ambient...
Topics
- Amino Acid Sequence
- Archaeal Proteins
- Bacterial Proteins
- Cloning, Molecular
- Crystallography, X-Ray
- Escherichia coli
- Gene Expression
- Kinetics
- Models, Molecular
- Mutation
- Plant Proteins
- Plasmids
- Protein Engineering