Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Bioinformatic tools uncover the C-terminal strand of Rubisco's large subunit as hot-spot for specificity-enhancing mutations.

FEBS letters - 20 Feb 2007

Burisch C, Wildner G F, Schlitter J

Abstract excerpt

Rubisco assumes the double role of accumulating biomass by fixing carbon dioxide to ribulose-1,5-bisphosphate and binding of molecular oxygen to the same substrate. The specificity factor of this mutually competitive activity, defined as the ratio of carboxylation to oxygenation efficiency, varies considerably for reasons which remain obscure. The explanation and the enhancement of specificity are of high...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Computer Simulation
Share to Conserved Sequence
Share to Mutant Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Subunits

Share to Ribulose-Bisphosphate Carboxylase

Share to Sequence Analysis, Protein

Share to Substrate Specificity

Share to Synechococcus

Source

Identifiers

PMID: 17274986
DOI: 10.1016/j.febslet.2007.01.043

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Bioinformatic tools uncover the C-terminal strand of Rubisco's large subunit as hot-spot for specificity-enhancing mutations.PMID 17274986Read ↗

An evolution-based analysis scheme to identify CO2/O2 specificity-determining factors for ribulose 1,5-bisphosphate carboxylase/oxygenase.Semantic proximity Read ↗

Surveying the expanding prokaryotic Rubisco multiverse.Semantic proximity Read ↗

Rubisco activase requires residues in the large subunit N terminus to remodel inhibited plant Rubisco.Semantic proximity Read ↗

Stability-activity tradeoffs constrain the adaptive evolution of RubisCO.Semantic proximity Read ↗

Directed Evolution of an Improved Rubisco; In Vitro Analyses to Decipher Fact from Fiction.Semantic proximity Read ↗

A map of the rubisco biochemical landscape.Semantic proximity Read ↗

Enhancing the Catalytic Activity of Thermococcus kodakarensis RuBisCo via Computer-Aided Rational Design.Semantic proximity Read ↗

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

An improved Escherichia coli screen for Rubisco identifies a protein-protein interface that can enhance CO2-fixation kinetics.Semantic proximity Read ↗

Structure-based catalytic optimization of a type III Rubisco from a hyperthermophile.Semantic proximity Read ↗

Plant-like substitutions in the large-subunit carboxy terminus of Chlamydomonas Rubisco increase CO2/O2 specificity.Semantic proximity Read ↗

Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.