ArticleDevelopment genes and evolution2004
Conservation of functional domain structure in bicarbonate-regulated "soluble" adenylyl cyclases in bacteria and eukaryotes.
Article in Development genes and evolution, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- The role of soluble adenylyl cyclase in sensing and regulating intracellular pH.Pflugers Archiv : European journal of physiology · 2024Review
- Bicarbonate Evokes Reciprocal Changes in Intracellular Cyclic di-GMP and Cyclic AMP Levels inBiology · 2021Article
- Multi-state design of flexible proteins predicts sequences optimal for conformational change.PLoS computational biology · 2020Article
- Comparative genomic analysis suggests that the sperm-specific sodium/proton exchanger and soluble adenylyl cyclase are key regulators of CatSper among the Metazoa.Zoological letters · 2019Article
- Cyanobacteriochrome-based photoswitchable adenylyl cyclases (cPACs) for broad spectrum light regulation of cAMP levels in cells.The Journal of biological chemistry · 2018Article
- Functional Significance of the Adcy10-Dependent Intracellular cAMP Compartments.Journal of cardiovascular development and disease · 2018Review
- The central role of cAMP in regulating Plasmodium falciparum merozoite invasion of human erythrocytes.PLoS pathogens · 2014Article
- Crystal structure of human soluble adenylate cyclase reveals a distinct, highly flexible allosteric bicarbonate binding pocket.ChemMedChem · 2014Article
- Crystal structures of human soluble adenylyl cyclase reveal mechanisms of catalysis and of its activation through bicarbonate.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Role of the bicarbonate-responsive soluble adenylyl cyclase in pH sensing and metabolic regulation.Frontiers in physiology · 2014Review
- High adenylyl cyclase activity and in vivo cAMP fluctuations in corals suggest central physiological role.Scientific reports · 2013Article
- Characterization of Plasmodium falciparum adenylyl cyclase-β and its role in erythrocytic stage parasites.PloS one · 2012Article
- Physiological sensing of carbon dioxide/bicarbonate/pH via cyclic nucleotide signaling.Sensors (Basel, Switzerland) · 2011Review
- Bicarbonate-sensing soluble adenylyl cyclase is an essential sensor for acid/base homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Stimulation of mammalian G-protein-responsive adenylyl cyclases by carbon dioxide.The Journal of biological chemistry · 2009Article
- Somatic 'soluble' adenylyl cyclase isoforms are unaffected in Sacy tm1Lex/Sacy tm1Lex 'knockout' mice.PloS one · 2008Article
- Molecular details of cAMP generation in mammalian cells: a tale of two systems.Journal of molecular biology · 2006Review
- Regulation of prokaryotic adenylyl cyclases by CO2.The Biochemical journal · 2006Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Soluble adenylyl cyclase (sAC) is an evolutionarily conserved bicarbonate sensor. In mammals, it is responsible for bicarbonate-induced, cAMP-dependent processes in sperm required for fertilization and postulated to be involved in other bicarbonate- and carbon dioxide-dependent functions throughout the body. Among eukaryotes, sAC-like cyclases have been detected in mammals and in the fungi Dictyostelium; these enzymes display extensive similarity extending through two cyclase catalytic domains and a long carboxy terminal extension. sAC-like cyclases are also found in a number of bacterial phyla (Cyanobacteria, Actinobacteria, and Proteobacteria), but these enzymes generally possess only a single catalytic domain and little, if any, homology with the remainder of the mammalian protein. Database mining through a number of recently sequenced genomes identified sAC orthologues in additional metazoan phyla (Arthropoda and Chordata) and additional bacterial phyla (Chloroflexi). Interestingly, the Chloroflexi sAC-like cyclases, a family of three enzymes from the thermophilic eubacterium, Chloroflexus aurantiacus, are more similar to eukaryotic sAC-like cyclases (i.e., mammalian sAC and Dictyostelium SgcA) than they are to other bacterial adenylyl cyclases (ACs) (i.e., from Cyanobacteria). The Chloroflexus sAC-like cyclases each possess two cyclase catalytic domains and extensive similarity with mammalian enzymes through their carboxy termini. We cloned one of the Chloroflexus sAC-like cyclases and confirmed it to be stimulated by bicarbonate. These data extend the family of organisms possessing bicarbonate-responsive ACs to numerous phyla within the bacterial and eukaryotic kingdoms.
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