ArticleJournal of bacteriology2002
Carbonic anhydrase is essential for growth of Ralstonia eutropha at ambient CO(2) concentrations.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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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.
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Who cites it
47 citing papers in PubMed, 116 citations in OpenAlex.
- Roles of three carbonic anhydrases inFEMS microbes · 2026Article
- Effects of COCurrent opinion in microbiology · 2024Review
- Widespread dissolved inorganic carbon-modifying toolkits in genomes of autotrophicApplied and environmental microbiology · 2024Review
- Microbial tapestry of the Shulgan-Tash cave (Southern Ural, Russia): influences of environmental factors on the taxonomic composition of the cave biofilms.Environmental microbiome · 2023Article
- Rational engineering of natural polyhydroxyalkanoates producing microorganisms for improved synthesis and recovery.Microbial biotechnology · 2023Review
- Carbonic Anhydrase Inhibitors as Novel Antibacterials in the Era of Antibiotic Resistance: Where Are We Now?Antibiotics (Basel, Switzerland) · 2023Review
- Trajectories for the evolution of bacterial COProceedings of the National Academy of Sciences of the United States of America · 2022Article
- The gram-negative bacteriumJournal of enzyme inhibition and medicinal chemistry · 2022Article
- Bis-pharmacophore of cinnamaldehyde-clubbed thiosemicarbazones as potent carbonic anhydrase-II inhibitors.Scientific reports · 2022Article
- Role of carbon-dioxide sequestering bacteria for clean air environment and prospective production of biomaterials: a sustainable approach.Environmental science and pollution research international · 2022Review
- Biosequestration of carbon dioxide using carbonic anhydrase from novel Streptomyces kunmingensis.Archives of microbiology · 2022Article
- The reliance of glycerol utilization by Cupriavidus necator on COApplied microbiology and biotechnology · 2022Article
- Carbonic Anhydrases: New Perspectives on Protein Functional Role and Inhibition inFrontiers in microbiology · 2021Review
- Article
- Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacteriumJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Genomic and Physiological Characteristics of a Novel Nitrite-OxidizingFrontiers in microbiology · 2020Article
- Phaeodactylum tricornutum as a model organism for testing the membrane penetrability of sulphonamide carbonic anhydrase inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2019Article
- The carbonic anhydrase of Clostridium autoethanogenum represents a new subclass of β-carbonic anhydrases.Applied microbiology and biotechnology · 2019Article
- Polymorphisms inFrontiers in microbiology · 2019Article
- Efficient biochemical production of acetoin from carbon dioxide usingBiotechnology for biofuels · 2019Article
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 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutant strain 25-1 of the facultative chemoautotroph Ralstonia eutropha H16 had previously been shown to exhibit an obligately high-CO(2)-requiring (HCR) phenotype. Although the requirement varied with the carbon and energy sources utilized, none of these conditions allowed growth at the air concentration of CO(2). In the present study, a gene designated can and encoding a beta-carbonic anhydrase (CA) was identified as the site altered in strain 25-1. The mutation caused a replacement of the highly conserved glycine residue 98 by aspartate in Can. A can deletion introduced into wild-type strain H16 generated mutant HB1, which showed the same HCR phenotype as mutant 25-1. Overexpression of can in Escherichia coli and mass spectrometric determination of CA activity demonstrated that can encodes a functional CA. The enzyme is inhibited by ethoxyzolamide and requires 40 mM MgSO(4) for maximal activity. Low but significant CA activities were detected in wild-type H16 but not in mutant HB1, strongly suggesting that the CA activity of Can is essential for growth of the wild type in the presence of low CO(2) concentrations. The HCR phenotype of HB1 was overcome by complementation with heterologous CA genes, indicating that growth of the organism at low CO(2) concentrations requires sufficient CA activity rather than the specific function of Can. The metabolic function(s) depending on CA activity remains to be identified.
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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.