ArticleThe Journal of biological chemistry2009
Substrate-induced assembly of Methanococcoides burtonii D-ribulose-1,5-bisphosphate carboxylase/oxygenase dimers into decamers.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 54 citations in OpenAlex.
- Chloroplasts and Plant Sustainability: Key Roles and Emerging Insights.International journal of molecular sciences · 2026Review
- Deep-branching evolutionary intermediates reveal structural origins of form I rubisco.Current biology : CB · 2023Article
- Structural plasticity enables evolution and innovation of RuBisCO assemblies.Science advances · 2022Article
- An Insight of RuBisCO Evolution through a Multilevel Approach.Biomolecules · 2021Article
- Novel bacterial clade reveals origin of form I Rubisco.Nature plants · 2020Article
- Molecular basis for the assembly of RuBisCO assisted by the chaperone Raf1.Nature plants · 2020Article
- The Prodigal Compound: Return of Ribosyl 1,5-Bisphosphate as an Important Player in Metabolism.Microbiology and molecular biology reviews : MMBR · 2019Review
- Lateral Gene Transfer Shapes the Distribution of RuBisCO among Candidate Phyla Radiation Bacteria and DPANN Archaea.Molecular biology and evolution · 2019Article
- A peptide adhesive molded by magnesium glues Rubisco's subunits together.The Journal of biological chemistry · 2017Article
- A unique structural domain inThe Journal of biological chemistry · 2017Article
- RubisCO of a nucleoside pathway known from Archaea is found in diverse uncultivated phyla in bacteria.The ISME journal · 2016Article
- RubisCO selection using the vigorously aerobic and metabolically versatile bacterium Ralstonia eutropha.The FEBS journal · 2016Article
- Evolving Methanococcoides burtonii archaeal Rubisco for improved photosynthesis and plant growth.Scientific reports · 2016Article
- In Vivo Studies in Rhodospirillum rubrum Indicate That Ribulose-1,5-bisphosphate Carboxylase/Oxygenase (Rubisco) Catalyzes Two Obligatorily Required and Physiologically Significant Reactions for Distinct Carbon and Sulfur Metabolic Pathways.The Journal of biological chemistry · 2015Article
- Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria.Nature communications · 2015Article
- A pentose bisphosphate pathway for nucleoside degradation in Archaea.Nature chemical biology · 2015Article
- Role of small subunit in mediating assembly of red-type form I Rubisco.The Journal of biological chemistry · 2015Article
- Substrate-Induced Dimerization of Engineered Monomeric Variants of Triosephosphate Isomerase from Trichomonas vaginalis.PloS one · 2015Article
- Article
- Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.Microbiology and molecular biology reviews : MMBR · 2014Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Like many enzymes, the biogenesis of the multi-subunit CO(2)-fixing enzyme ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) in different organisms requires molecular chaperones. When expressed in Escherichia coli, the large (L) subunits of the Rubisco from the archaeabacterium Methanococcoides burtonii assemble into functional dimers (L(2)). However, further assembly into pentamers of L(2) (L(10)) occurs when expressed in tobacco chloroplasts or E. coli producing RuBP. In vitro analyses indicate that the sequential assembly of L(2) into L(10) (via detectable L(4) and L(6) intermediates) occurs without chaperone involvement and is stimulated by protein rearrangements associated with either the binding of substrate RuBP, the tight binding transition state analog carboxyarabinitol-1,5-bisphosphate, or inhibitory divalent metal ions within the active site. The catalytic properties of L(2) and L(10) M. burtonii Rubisco (MbR) were indistinguishable. At 25 degrees C they both shared a low specificity for CO(2) over O(2) (1.1 mol x mol(-1)) and RuBP carboxylation rates that were distinctively enhanced at low pH (approximately 4 s(-1) at pH 6, relative to 0.8 s(-1) at pH 8) with a temperature optimum of 55 degrees C. Like other archaeal Rubiscos, MbR also has a high O(2) affinity (K(m)(O(2)) = approximately 2.5 microM). The catalytic and structural similarities of MbR to other archaeal Rubiscos contrast with its closer sequence homology to bacterial L(2) Rubisco, complicating its classification within the Rubisco superfamily.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.