Reversible hydration of carbon dioxide (Homo sapiens)

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6, 20, 22, 25, 395, 7, 11, 14, 16...1, 2, 8-10, 12...5, 7, 11, 14, 16...19, 25, 29, 401, 2, 8-10, 12...3, 4, 18, 25, 32...19, 25, 29, 403, 4, 18, 25, 32...CA7:Zinc [cytosol]CA6:Zinc[extracellularregion]cytosolCA5B:Zinc[mitochondrialmatrix]CA5A/B:Zinc[mitochondrialmatrix]CA12 Dimer:Zinc[plasma membrane]CA13:Zinc [cytosol]CA9:Zinc [plasmamembrane]mitochondrial matrixCA1:Zn2+ [cytosol]CA5A:Zinc[mitochondrialmatrix]CA14:Zinc [plasmamembrane]CA1/2/3/7/13:Zinc[cytosol]CA2:Zn2+ [cytosol]CA4:Zn2+ [plasmamembrane]CA12:Zinc [plasmamembrane]CA3:Zinc [cytosol]CA4/9/14/12:Zinc[plasma membrane,extracellularregion]CA2 [cytosol]CA7 [cytosol]Zn2+ [extracellularregion]HCO3-CO2CO2H2OCA14 [plasmamembrane]N-seryl-glycosylphosphatidylinositolethanolamine-CA4[plasma membrane]CO2Zn2+ [cytosol]CA1 [cytosol]H+CA13 [cytosol]Zn2+ [mitochondrialmatrix]CA5A/B:ZincHCO3-H2OCA6 [extracellularregion]CA9 [plasmamembrane]CA4/9/14/12:ZincCA12 [plasmamembrane]CA5A [mitochondrialmatrix]CA5B [mitochondrialmatrix]H+HCO3-Zn2+ [extracellularregion]H+CA3 [cytosol]H2OCA6:ZincCA1/2/3/7/13:Zinc14


Description

Carbonic anhydrases reversibly catalyze the hydration of carbon dioxide and directly produce bicarbonate and protons, bypassing the formation of carbonic acid (reviewed in Lindskog 1997, Breton 2001, Esbaugh and Tufts 2006, Boron 2010, Gilmour 2010). 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. There are currently 12 known active carbonic anhydrases in humans.Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=1475029

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Bibliography

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  2. Fujikawa-Adachi K, Nishimori I, Taguchi T, Onishi S.; ''Human mitochondrial carbonic anhydrase VB. cDNA cloning, mRNA expression, subcellular localization, and mapping to chromosome x.''; PubMed Europe PMC Scholia
  3. Bootorabi F, Jänis J, Smith E, Waheed A, Kukkurainen S, Hytönen V, Valjakka J, Supuran CT, Vullo D, Sly WS, Parkkila S.; ''Analysis of a shortened form of human carbonic anhydrase VII expressed in vitro compared to the full-length enzyme.''; PubMed Europe PMC Scholia
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  5. Silverman DN, Tu C, Chen X, Tanhauser SM, Kresge AJ, Laipis PJ.; ''Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase III.''; PubMed Europe PMC Scholia
  6. Nishimori I, Innocenti A, Vullo D, Scozzafava A, Supuran CT.; ''Carbonic anhydrase inhibitors: the inhibition profiles of the human mitochondrial isoforms VA and VB with anions are very different.''; PubMed Europe PMC Scholia
  7. Khalifah RG.; ''The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C.''; PubMed Europe PMC Scholia
  8. Nishimori I, Minakuchi T, Onishi S, Vullo D, Scozzafava A, Supuran CT.; ''Carbonic anhydrase inhibitors. DNA cloning, characterization, and inhibition studies of the human secretory isoform VI, a new target for sulfonamide and sulfamate inhibitors.''; PubMed Europe PMC Scholia
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  31. Ulmasov B, Waheed A, Shah GN, Grubb JH, Sly WS, Tu C, Silverman DN.; ''Purification and kinetic analysis of recombinant CA XII, a membrane carbonic anhydrase overexpressed in certain cancers.''; PubMed Europe PMC Scholia
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  34. Ren X, Lindskog S.; ''Buffer dependence of CO2 hydration catalyzed by human carbonic anhydrase I.''; PubMed Europe PMC Scholia
  35. Pesando JM.; ''Proton magnetic resonance studies of carbonic anhydrase. II. Group controlling catalytic activity.''; PubMed Europe PMC Scholia
  36. Pastorekova S, Vullo D, Nishimori I, Scozzafava A, Pastorek J, Supuran CT.; ''Carbonic anhydrase activators: activation of the human tumor-associated isozymes IX and XII with amino acids and amines.''; PubMed Europe PMC Scholia
  37. Thatcher BJ, Doherty AE, Orvisky E, Martin BM, Henkin RI.; ''Gustin from human parotid saliva is carbonic anhydrase VI.''; PubMed Europe PMC Scholia
  38. 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.; ''Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes.''; PubMed Europe PMC Scholia
  39. Jones GL, Shaw DC.; ''A chemical and enzymological comparison of the common major human erythrocyte carbonic anhydrase II, its minor component, and a new genetic variant, CA II Melbourne (237 Pro leads to His).''; PubMed Europe PMC Scholia
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  41. Ozensoy O, Nishimori I, Vullo D, Puccetti L, Scozzafava A, Supuran CT.; ''Carbonic anhydrase inhibitors: inhibition of the human transmembrane isozyme XIV with a library of aromatic/heterocyclic sulfonamides.''; PubMed Europe PMC Scholia

History

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114783view16:27, 25 January 2021ReactomeTeamReactome version 75
113228view11:29, 2 November 2020ReactomeTeamReactome version 74
112450view15:39, 9 October 2020ReactomeTeamReactome version 73
101357view11:24, 1 November 2018ReactomeTeamreactome version 66
100895view20:59, 31 October 2018ReactomeTeamreactome version 65
100436view19:33, 31 October 2018ReactomeTeamreactome version 64
99985view16:17, 31 October 2018ReactomeTeamreactome version 63
99539view14:52, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99174view12:42, 31 October 2018ReactomeTeamreactome version 62
93748view13:33, 16 August 2017ReactomeTeamreactome version 61
93267view11:18, 9 August 2017ReactomeTeamreactome version 61
89078view06:09, 22 August 2016EgonwOntology Term : 'classic metabolic pathway' added !
86344view09:15, 11 July 2016ReactomeTeamreactome version 56
83176view10:17, 18 November 2015ReactomeTeamVersion54
81773view10:22, 26 August 2015ReactomeTeamVersion53
77043view08:34, 17 July 2014ReactomeTeamFixed remaining interactions
76748view12:11, 16 July 2014ReactomeTeamFixed remaining interactions
76073view10:13, 11 June 2014ReactomeTeamRe-fixing comment source
75783view11:31, 10 June 2014ReactomeTeamReactome 48 Update
75133view14:08, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74780view08:52, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
CA1 [cytosol]ProteinP00915 (Uniprot-TrEMBL)
CA1/2/3/7/13:ZincComplexREACT_122866 (Reactome)
CA12 [plasma membrane]ProteinO43570 (Uniprot-TrEMBL)
CA13 [cytosol]ProteinQ8N1Q1 (Uniprot-TrEMBL)
CA14 [plasma membrane]ProteinQ9ULX7 (Uniprot-TrEMBL)
CA2 [cytosol]ProteinP00918 (Uniprot-TrEMBL)
CA3 [cytosol]ProteinP07451 (Uniprot-TrEMBL)
CA4/9/14/12:ZincComplexREACT_123111 (Reactome)
CA5A [mitochondrial matrix]ProteinP35218 (Uniprot-TrEMBL)
CA5A/B:ZincComplexREACT_125046 (Reactome)
CA5B [mitochondrial matrix]ProteinQ9Y2D0 (Uniprot-TrEMBL)
CA6 [extracellular region]ProteinP23280 (Uniprot-TrEMBL)
CA6:ZincComplexREACT_124884 (Reactome)
CA7 [cytosol]ProteinP43166 (Uniprot-TrEMBL)
CA9 [plasma membrane]ProteinQ16790 (Uniprot-TrEMBL)
CO2MetaboliteCHEBI:16526 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HCO3-MetaboliteCHEBI:17544 (ChEBI)
N-seryl-glycosylphosphatidylinositolethanolamine-CA4 [plasma membrane]ProteinP22748 (Uniprot-TrEMBL)
Zn2+ [cytosol]MetaboliteCHEBI:29105 (ChEBI)
Zn2+ [extracellular region]MetaboliteCHEBI:29105 (ChEBI)
Zn2+ [mitochondrial matrix]MetaboliteCHEBI:29105 (ChEBI)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
CA1/2/3/7/13:Zincmim-catalysisREACT_120719 (Reactome)
CA1/2/3/7/13:Zincmim-catalysisREACT_120951 (Reactome)
CA4/9/14/12:Zincmim-catalysisREACT_120844 (Reactome)
CA4/9/14/12:Zincmim-catalysisREACT_121310 (Reactome)
CA5A/B:Zincmim-catalysisREACT_120901 (Reactome)
CA5A/B:Zincmim-catalysisREACT_120942 (Reactome)
CA6:Zincmim-catalysisREACT_120791 (Reactome)
CA6:Zincmim-catalysisREACT_120867 (Reactome)
CO2ArrowREACT_120719 (Reactome)
CO2ArrowREACT_120791 (Reactome)
CO2ArrowREACT_120844 (Reactome)
CO2ArrowREACT_120942 (Reactome)
CO2REACT_120867 (Reactome)
CO2REACT_120901 (Reactome)
CO2REACT_120951 (Reactome)
CO2REACT_121310 (Reactome)
H+ArrowREACT_120867 (Reactome)
H+ArrowREACT_120901 (Reactome)
H+ArrowREACT_120951 (Reactome)
H+ArrowREACT_121310 (Reactome)
H+REACT_120719 (Reactome)
H+REACT_120791 (Reactome)
H+REACT_120844 (Reactome)
H+REACT_120942 (Reactome)
H2OArrowREACT_120719 (Reactome)
H2OArrowREACT_120791 (Reactome)
H2OArrowREACT_120844 (Reactome)
H2OArrowREACT_120942 (Reactome)
H2OREACT_120867 (Reactome)
H2OREACT_120901 (Reactome)
H2OREACT_120951 (Reactome)
H2OREACT_121310 (Reactome)
HCO3-ArrowREACT_120867 (Reactome)
HCO3-ArrowREACT_120901 (Reactome)
HCO3-ArrowREACT_120951 (Reactome)
HCO3-ArrowREACT_121310 (Reactome)
HCO3-REACT_120719 (Reactome)
HCO3-REACT_120791 (Reactome)
HCO3-REACT_120844 (Reactome)
HCO3-REACT_120942 (Reactome)
REACT_120719 (Reactome) Carbonic anhydrase I (CA1, Khalifah 1971, Simonsson et al. 1982, Ren and Lindskog 1992), carbonic anyhydrase II (CA2, Tibell et al. 1984, Jones and Shaw 1983, Pesando 1975, Ghannam et al. 1986), carbonic anhydrase III (CA3, Carter et al. 1979, Tu et al. 1990, Tu et al. 1994, Tu et al. 1998, Silverman et al. 1993), carbonic anhydrase VII (CA7, Bootorabi et al. 2010, Gitto et al. 2010) dehydrate cytosolic bicarbonate to yield water and carbon dioxide (reviewed in Lindskog 1997). Depending on the concentrations of reactants the reaction is reversible.
CA2 and CA7 have high catalytic activity, CA1 has low activity (10% of the activity of CA2), and CA3 has very low activity (1% of the activity of CA2). CA1 and CA2 are found in erythrocytes. CA2 is also found in kidney, lung, and white muscle where it facilitates diffusion of carbon dioxide. CA3 is found in red muscle where it participates in resistance against oxidative stress.
REACT_120791 (Reactome) Carbonic anhydrase VI (CA6) dehydrates bicarbonate to yield water and carbon dioxide (Thatcher et al. 1998, Nishimori et al. 2007). Depending on the concentrations of reactants the reaction is reversible. CA6 is a major protein of saliva and is also known as gustin.
REACT_120844 (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 (CA14, Ozensoy et al. 2005, Temperini et al. 2008) are membrane-bound enzymes that dehydrate bicarbonate to yield water and carbon dioxide. Depending on the concentrations of reactants the reaction is reversible.
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.
REACT_120867 (Reactome) Carbonic anhydrase VI (CA6) hydrates carbon dioxide to yield bicarbonate and a proton (Thatcher et al. 1998, Nishimori et al. 2007).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. CA6 is a major protein of saliva and is also known as gustin.
REACT_120901 (Reactome) Carbonic anhydrase VA (CA5A, Nagao et al. 1993, Franchi et al. 2003, Nishimori et al. 2007) and carbonic anhydrase VB (CA5B, Fujikawa-Adachi et al. 1999, Nishimori et al. 2005, Nishimori et al. 2007) hydrate carbon dioxide in mitochondria 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.
REACT_120942 (Reactome) Carbonic anhydrase VA (CA5A, Nagao et al. 1993, Franchi et al. 2003, Nishimori et al. 2007) and carbonic anhydrase VB (CA5B, Fujikawa-Adachi et al. 1999, Nishimori et al. 2005, Nishimori et al. 2007) dehydrate bicarbonate in mitochondria to yield water and carbon dioxide (reviewed in Lindskog 1997). Depending on the concentrations of reactants the reaction is reversible.
REACT_120951 (Reactome) Carbonic anhydrase I (CA1, Khalifah 1971, Simonsson et al. 1982, Ren and Lindskog 1992), carbonic anyhydrase II (CA2, Tibell et al. 1984, Jones and Shaw 1983, Pesando 1975, Ghannam et al. 1986), carbonic anhydrase III (CA3, Carter et al. 1979, Tu et al. 1990, Tu et al. 1994, Tu et al. 1998, Silverman et al. 1993), carbonic anhydrase VII (CA7, Bootorabi et al. 2010, Gitto et al. 2010) hydrate 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.
CA2 and CA7 have high catalytic activity, CA1 has low activity (10% of the activity of CA2), and CA3 has very low activity (1% of the activity of CA2). CA1 and CA2 are found in erythrocytes. CA2 is also found in kidney, lung, and white muscle where it facilitates diffusion of carbon dioxide. CA3 is found in red muscle where it participates in resistance against oxidative stress.
REACT_121310 (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.
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.
Retrieved from "https://classic.wikipathways.org/index.php/Pathway:WP2770"
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