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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...

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Identifiers

PMID: 27273261
DOI: 10.1002/prot.25080

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Mutation design of a thermophilic Rubisco based on three-dimensional structure enhances its activity at ambient temperature.PMID 27273261Read ↗

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