BioPAX pathway converted from "Carbonic anhydrase hydrates carbon dioxide (plasma membrane)" in the Reactome database. Carbonic anhydrase hydrates carbon dioxide (plasma membrane) Carbonic anhydrase hydrates carbon dioxide (plasma membrane) This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='' target='NEW'></a> Reactome DB_ID: 109276 1 extracellular region GO 0005576 water [ChEBI:15377] water Reactome ChEBI 15377 Reactome DB_ID: 1237009 1 carbon dioxide [ChEBI:16526] carbon dioxide ChEBI 16526 Reactome DB_ID: 351626 1 hydron [ChEBI:15378] hydron ChEBI 15378 Reactome DB_ID: 425425 1 hydrogencarbonate [ChEBI:17544] hydrogencarbonate ChEBI 17544 PHYSIOL-LEFT-TO-RIGHT ACTIVATION Converted from EntitySet in Reactome Reactome DB_ID: 10409131 plasma membrane GO 0005886 CA4,9,14,12:Zn2+ [plasma membrane] Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntity GO 0004089 GO molecular function Reactome Database ID Release 83 10409132 Database identifier. Use this URL to connect to the web page of this instance in Reactome: Reactome Database ID Release 83 10409169 Database identifier. Use this URL to connect to the web page of this instance in Reactome: Reactome R-DRE-1475025 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: Carbonic anhydrase IV (CA4, Zhu and Sly 1990, Okuyama et al. 1992, Baird et al. 1997, Innocenti et al. 2004), carbonic anhydrase IX (CA9, Wingo et al. 2001, Hilvo et al. 2008), carbonic anhydrase XII (CA12, Ulmasov et al. 2000, Pastorekova et al. 2008), and carbonic anhydrase XIV (CA14Ozensoy et al. 2005, Temperini et al. 2008) are membrane-bound enzymes that hydrate extracellular carbon dioxide to yield bicarbonate and a proton.Carbonic anhydrase deprotonates water to yield a zinc-hydroxyl group and a proton which is transferred to external buffer molecules via histidine or glutamate residues in carbonic anhydrase. The hydroxyl group reacts with carbon dioxide in the active site to yield bicarbonate. A water molecule displaces the bicarbonate and the reaction cycle begins again (reviewed in Lindskog 1997). Depending on the concentrations of reactants the reaction is reversible.<br>CA4 has high catalytic activity. CA9, CA12, and CA14 have moderate activity. CA4 is anchored to the extracellular face of the plasma membrane by glycosylphosphatidylinositol. CA9, CA12, and CA14 are single-pass transmembrane proteins. CA4 is found on the extracellular face of capillaries in kidney, lung, and muscle where it maintains the gradient of carbon dioxide between tissue and blood. CA9 and CA12 are found on basolateral membranes of epithelia. CA9 is inducible by Hypoxia-inducible factor 1 alpha (HIF1alpha) and acidifies the extracellular environment of tumors. In rodents CA15 is membrane anchored and has low activity; in primates CA15 is a pseudogene. 2111324 Pubmed 1990 Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidney Zhu, XL Sly, William S J Biol Chem 265:8795-801 18294854 Pubmed 2008 Carbonic anhydrase activators: activation of the human tumor-associated isozymes IX and XII with amino acids and amines Pastorekova, S Vullo, D Nishimori, I Scozzafava, A Pastorek, J Supuran, CT Bioorg Med Chem 16:3530-6 15501038 Pubmed 2004 Carbonic anhydrase inhibitors: inhibition of the membrane-bound human isozyme IV with anions Innocenti, A Firnges, MA Antel, J Wurl, M Scozzafava, A Supuran, CT Bioorg Med Chem Lett 14:5769-73 11676494 Pubmed 2001 The catalytic properties of human carbonic anhydrase IX Wingo, T Tu, C Laipis, PJ Silverman, DN Biochem Biophys Res Commun 288:666-9 9054574 Pubmed 1997 Catalysis and inhibition of human carbonic anhydrase IV Baird TT, Jr Waheed, A Okuyama, T Sly, William S Fierke, CA Biochemistry 36:2669-78 18162396 Pubmed 2008 Carbonic anhydrase inhibitors. Interaction of 2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide with 12 mammalian isoforms: kinetic and X-ray crystallographic studies Temperini, C Cecchi, A Boyle, NA Scozzafava, A Cabeza, JE Wentworth P, Jr Blackburn, GM Supuran, CT Bioorg Med Chem Lett 18:999-1005 16006130 Pubmed 2005 Carbonic anhydrase inhibitors: inhibition of the human transmembrane isozyme XIV with a library of aromatic/heterocyclic sulfonamides Ozensoy, O Nishimori, I Vullo, D Puccetti, L Scozzafava, A Supuran, CT Bioorg Med Chem 13:6089-93 9336012 Pubmed 1997 Structure and mechanism of carbonic anhydrase Lindskog, S Pharmacol Ther 74:1-20 7625839 Pubmed 1995 Carbonic anhydrase IV: role of removal of C-terminal domain in glycosylphosphatidylinositol anchoring and realization of enzyme activity Okuyama, T Waheed, A Kusumoto, W Zhu, XL Sly, William S Arch Biochem Biophys 320:315-22 18703501 Pubmed 2008 Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes Hilvo, M Baranauskiene, L Salzano, AM Scaloni, A Matulis, D Innocenti, A Scozzafava, A Monti, SM Di Fiore, A De Simone, G Lindfors, M Jänis, J Valjakka, J Pastoreková, S Pastorek, J Kulomaa, MS Nordlund, HR Supuran, CT Parkkila, S J Biol Chem 283:27799-809 11121027 Pubmed 2000 Purification and kinetic analysis of recombinant CA XII, a membrane carbonic anhydrase overexpressed in certain cancers Ulmasov, B Waheed, A Shah, GN Grubb, JH Sly, William S Tu, C Silverman, DN Proc Natl Acad Sci U S A 97:14212-7 inferred by electronic annotation IEA GO IEA