ArticleThe EMBO journal2000
The active site architecture of Pisum sativum beta-carbonic anhydrase is a mirror image of that of alpha-carbonic anhydrases.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 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
81 citing papers in PubMed, 283 citations in OpenAlex.
- Structural insights into the coupling mechanism of vectorial COProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Fungal Carbonic Anhydrases: A Systematic Review from Molecular Profiling to Pathogenic Regulation inJournal of fungi (Basel, Switzerland) · 2026Review
- How far can you go? Extrapolating values of catalytic activity from known protein landscapes in natural and directed evolution.Chemical Society reviews · 2026Review
- A Novel Strategy for Highly Efficient Heterologous Expression of Carbonic Anhydrase inInternational journal of molecular sciences · 2026Article
- Structural basis of membrane potential coupled vectorial CO₂ hydration by the DAB2 complex in chemolithoautotrophs.Nature communications · 2026Article
- A guard cell carbonic anhydrase binds and regulates SLAC1 separate from its catalytic activity.Nature communications · 2026Article
- Deep models of protein evolution in time generate realistic evolutionary trajectories and functional proteins.bioRxiv : the preprint server for biology · 2026Article
- Recent insights into α-carboxysome structure, mechanism, and assembly.Journal of bacteriology · 2026Review
- Introduction to Carbonic Anhydrase.Sub-cellular biochemistry · 2026Review
- Structure and encapsulation of carbonic anhydrase within the α-carboxysome.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Characterization of fungal carbonyl sulfide hydrolase belonging to clade D β-carbonic anhydrase.FEBS letters · 2025Article
- Carbonic Anhydrases: Different Active Sites, Same Metal Selectivity Rules.Molecules (Basel, Switzerland) · 2024Article
- Expression and localization of two β-carbonic anhydrases inFrontiers in plant science · 2024Article
- Cloning, characterization, and inhibition of the novel β-carbonic anhydrase from parasitic blood fluke,Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminthJournal of enzyme inhibition and medicinal chemistry · 2022Article
- Arabidopsis plastid carbonic anhydrase βCA5 is important for normal plant growth.Plant physiology · 2022Article
- α-CAs from Photosynthetic Organisms.International journal of molecular sciences · 2022Review
- Emerging trends in environmental and industrial applications of marine carbonic anhydrase: a review.Bioprocess and biosystems engineering · 2022Review
- Contribution of the Mitochondrial Carbonic Anhydrase (MoCA1) to Conidiogenesis and Pathogenesis inFrontiers in microbiology · 2022Article
- Activation of the β-carbonic anhydrase from the protozoan pathogenJournal of enzyme inhibition and medicinal chemistry · 2021Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have determined the structure of the beta-carbonic anhydrase from the dicotyledonous plant Pisum sativum at 1.93 A resolution, using a combination of multiple anomalous scattering off the active site zinc ion and non-crystallographic symmetry averaging. The mol- ecule assembles as an octamer with a novel dimer of dimers of dimers arrangement. Two distinct patterns of conservation of active site residues are observed, implying two potentially mechanistically distinct classes of beta-carbonic anhydrases. The active site is located at the interface between two monomers, with Cys160, His220 and Cys223 binding the catalytic zinc ion and residues Asp162 (oriented by Arg164), Gly224, Gln151, Val184, Phe179 and Tyr205 interacting with the substrate analogue, acetic acid. The substrate binding groups have a one to one correspondence with the functional groups in the alpha-carbonic anhydrase active site, with the corresponding residues being closely superimposable by a mirror plane. Therefore, despite differing folds, alpha- and beta-carbonic anhydrase have converged upon a very similar active site design and are likely to share a common mechanism.
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.