Reversible hydration of carbon dioxide (Homo sapiens)

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5, 9, 22, 32, 396, 10, 12, 20-221, 3, 4, 7, 11...1, 3, 4, 7, 11...22, 28, 31, 412, 8, 13, 14, 17...2, 8, 13, 14, 17...6, 10, 12, 20-2222, 28, 31, 41cytosolmitochondrial matrixCA3 CA13 CA9 CA1,2,3,7,13:ZincH2OHCO3-H+CA12 H2OZn2+ H+CA2 Zn2+ CA5A,B:ZincCO2CA5B CA5A CA4,9,14,12:ZincZn2+ CA14 N-seryl-glycosylphosphatidylinositolethanolamine-CA4 H2OZn2+ CO2CA6:ZincHCO3-H+HCO3-CA7 CO2CA6 CA1 40


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. View original pathway at:Reactome.

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Bibliography

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  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
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History

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CompareRevisionActionTimeUserComment
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 ProteinP00915 (Uniprot-TrEMBL)
CA1,2,3,7,13:ZincComplexR-HSA-1475034 (Reactome)
CA12 ProteinO43570 (Uniprot-TrEMBL)
CA13 ProteinQ8N1Q1 (Uniprot-TrEMBL)
CA14 ProteinQ9ULX7 (Uniprot-TrEMBL)
CA2 ProteinP00918 (Uniprot-TrEMBL)
CA3 ProteinP07451 (Uniprot-TrEMBL)
CA4,9,14,12:ZincComplexR-HSA-1475027 (Reactome)
CA5A ProteinP35218 (Uniprot-TrEMBL)
CA5A,B:ZincComplexR-HSA-1475016 (Reactome)
CA5B ProteinQ9Y2D0 (Uniprot-TrEMBL)
CA6 ProteinP23280 (Uniprot-TrEMBL)
CA6:ZincComplexR-HSA-1237316 (Reactome)
CA7 ProteinP43166 (Uniprot-TrEMBL)
CA9 ProteinQ16790 (Uniprot-TrEMBL)
CO2MetaboliteCHEBI:16526 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HCO3-MetaboliteCHEBI:17544 (ChEBI)
N-seryl-glycosylphosphatidylinositolethanolamine-CA4 ProteinP22748 (Uniprot-TrEMBL)
Zn2+ MetaboliteCHEBI:29105 (ChEBI)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
CA1,2,3,7,13:Zincmim-catalysisR-HSA-1475022 (Reactome)
CA1,2,3,7,13:Zincmim-catalysisR-HSA-1475026 (Reactome)
CA4,9,14,12:Zincmim-catalysisR-HSA-1475017 (Reactome)
CA4,9,14,12:Zincmim-catalysisR-HSA-1475025 (Reactome)
CA5A,B:Zincmim-catalysisR-HSA-1475028 (Reactome)
CA5A,B:Zincmim-catalysisR-HSA-1475032 (Reactome)
CA6:Zincmim-catalysisR-HSA-1237045 (Reactome)
CA6:Zincmim-catalysisR-HSA-1237081 (Reactome)
CO2ArrowR-HSA-1237081 (Reactome)
CO2ArrowR-HSA-1475017 (Reactome)
CO2ArrowR-HSA-1475022 (Reactome)
CO2ArrowR-HSA-1475028 (Reactome)
CO2R-HSA-1237045 (Reactome)
CO2R-HSA-1475025 (Reactome)
CO2R-HSA-1475026 (Reactome)
CO2R-HSA-1475032 (Reactome)
H+ArrowR-HSA-1237045 (Reactome)
H+ArrowR-HSA-1475025 (Reactome)
H+ArrowR-HSA-1475026 (Reactome)
H+ArrowR-HSA-1475032 (Reactome)
H+R-HSA-1237081 (Reactome)
H+R-HSA-1475017 (Reactome)
H+R-HSA-1475022 (Reactome)
H+R-HSA-1475028 (Reactome)
H2OArrowR-HSA-1237081 (Reactome)
H2OArrowR-HSA-1475017 (Reactome)
H2OArrowR-HSA-1475022 (Reactome)
H2OArrowR-HSA-1475028 (Reactome)
H2OR-HSA-1237045 (Reactome)
H2OR-HSA-1475025 (Reactome)
H2OR-HSA-1475026 (Reactome)
H2OR-HSA-1475032 (Reactome)
HCO3-ArrowR-HSA-1237045 (Reactome)
HCO3-ArrowR-HSA-1475025 (Reactome)
HCO3-ArrowR-HSA-1475026 (Reactome)
HCO3-ArrowR-HSA-1475032 (Reactome)
HCO3-R-HSA-1237081 (Reactome)
HCO3-R-HSA-1475017 (Reactome)
HCO3-R-HSA-1475022 (Reactome)
HCO3-R-HSA-1475028 (Reactome)
R-HSA-1237045 (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.
R-HSA-1237081 (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.
R-HSA-1475017 (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.
R-HSA-1475022 (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.
R-HSA-1475025 (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.
R-HSA-1475026 (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.
R-HSA-1475028 (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.
R-HSA-1475032 (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.
Retrieved from "https://classic.wikipathways.org/index.php/Pathway:WP2770"
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