ArticleThe Journal of biological chemistry2009
Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism.
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 39 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
39 citing papers in PubMed, 85 citations in OpenAlex.
- Putative Mechanisms for Initial Reaction of Anaerobic Benzene Degradation Presumably Involving a Flavoprotein.Environmental microbiology · 2026Article
- Propionic acidemia in Mexico: Clinical and genotypic spectrum.Molecular genetics and metabolism reports · 2026Article
- Oligomeric assemblies of plant biotin carboxylase revealed by cryo-EM and cross-linking.The Biochemical journal · 2026Article
- A Novel β/ε Subunit Combination Expands the Tri-Subunit Acyl-CoA Carboxylase Repertoire inMicroorganisms · 2026Article
- Structural insight into synergistic activation of human 3-methylcrotonyl-CoA carboxylase.Nature structural & molecular biology · 2025Article
- Filament structures unveil the dynamic organization of human acetyl-CoA carboxylase.Science advances · 2024Article
- The cryo-EM structure of trypanosome 3-methylcrotonyl-CoA carboxylase provides mechanistic and dynamic insights into its enzymatic function.Structure (London, England : 1993) · 2024Article
- Article
- Widespread dissolved inorganic carbon-modifying toolkits in genomes of autotrophicApplied and environmental microbiology · 2024Review
- CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase.Nature communications · 2022Article
- Catalytic and structural properties of ATP-dependent caprolactamase from Pseudomonas jessenii.Proteins · 2021Article
- Rethinking the Citric Acid Cycle: Connecting Pyruvate Carboxylase and Citrate Synthase to the Flow of Energy and Material.International journal of molecular sciences · 2021Review
- MpsAB is important for Staphylococcus aureus virulence and growth at atmospheric CONature communications · 2019Article
- Crystal structure of the essential biotin-dependent carboxylase AccA3 fromFEBS open bio · 2017Article
- The Highly Conserved Asp23 Family Protein YqhY Plays a Role in Lipid Biosynthesis inFrontiers in microbiology · 2017Article
- Fungal naphtho-γ-pyrones: Potent antibiotics for drug-resistant microbial pathogens.Scientific reports · 2016Article
- Article
- Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase.Biochemistry · 2015Article
- Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase.Nature · 2015Article
- Enzymatic strategies and biocatalysts for amide bond formation: tricks of the trade outside of the ribosome.Molecular bioSystems · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Biotin-dependent carboxylases are widely distributed in nature and have important functions in many cellular processes. These enzymes share a conserved biotin carboxylase (BC) component, which catalyzes the ATP-dependent carboxylation of biotin using bicarbonate as the donor. Despite the availability of a large amount of biochemical and structural information on BC, the molecular basis for its catalysis is currently still poorly understood. We report here the crystal structure at 2.0 A resolution of wild-type Escherichia coli BC in complex with its substrates biotin, bicarbonate, and Mg-ADP. The structure suggests that Glu(296) is the general base that extracts the proton from bicarbonate, and Arg(338) is the residue that stabilizes the enolate biotin intermediate in the carboxylation reaction. The B domain of BC is positioned closer to the active site, leading to a 2-A shift in the bound position of the adenine nucleotide and bringing it near the bicarbonate for catalysis. One of the oxygen atoms of bicarbonate is located in the correct position to initiate the nucleophilic attack on ATP to form the carboxyphosphate intermediate. This oxygen is also located close to the N1' atom of biotin, providing strong evidence that the phosphate group, derived from decomposition of carboxyphosphate, is the general base that extracts the proton on this N1' atom. The structural observations are supported by mutagenesis and kinetic studies. Overall, this first structure of BC in complex with substrates offers unprecedented insights into the molecular mechanism for the catalysis by this family of enzymes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.