BioPAX pathway converted from "Reversible hydration of carbon dioxide" in the Reactome database.

Reversible hydration of carbon dioxide

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.

Authored: May, B, 2011-08-06Reviewed: Jassal, B, 2012-05-16Reviewed: Silverman, DN, 2012-05-16Edited: May, B, 2011-08-06

4.2.1.1

Carbonic anhydrase hydrates carbon dioxide (cytosol)

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.<br>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.

Authored: May, B, 2011-08-06Reviewed: Jassal, B, 2012-05-16Reviewed: Silverman, DN, 2012-05-16Edited: May, B, 2011-08-06

Reactome DB_ID: 113528

cytosolGO0005829

carbon dioxide [ChEBI:16526]

carbon dioxide

Reactomehttp://www.reactome.orgChEBI16526

Reactome DB_ID: 29356

water [ChEBI:15377]

water

ChEBI15377

Reactome DB_ID: 111627

hydrogencarbonate [ChEBI:17544]

hydrogencarbonate

ChEBI17544

Reactome DB_ID: 70106

hydron [ChEBI:15378]

hydron

ChEBI15378PHYSIOL-LEFT-TO-RIGHT

ACTIVATION

Converted from EntitySet in Reactome

Reactome DB_ID: 1475034

CA1,2,3,7,13:Zinc [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntity

GO0004089

GO molecular function

Reactome Database ID Release 751475014Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1475014Reactome Database ID Release 751475026Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1475026ReactomeR-HSA-1475026

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-1475026.22169869Pubmed1990Buffer enhancement of proton transfer in catalysis by human carbonic anhydrase IIITu, CKParanawithana, SRJewell, DATanhauser, SMLoGrasso, PVWynns, GCLaipis, PJSilverman, DNBiochemistry 29:6400-59336012Pubmed1997Structure and mechanism of carbonic anhydraseLindskog, SPharmacol Ther 74:1-206407977Pubmed1983A 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)Jones, GLShaw, DCHum Genet 63:392-920493921Pubmed2010Analysis of a shortened form of human carbonic anhydrase VII expressed in vitro compared to the full-length enzymeBootorabi, FJänis, JSmith, EWaheed, AKukkurainen, SHytönen, VValjakka, JSupuran, CTVullo, DSly, William SParkkila, SBiochimie 92:1072-803080418Pubmed1986Activation parameters for the carbonic anhydrase II-catalyzed hydration of CO2Ghannam, AFTsen, WRowlett, RSJ Biol Chem 261:1164-99635771Pubmed1998Properties of intramolecular proton transfer in carbonic anhydrase IIITu, CQian, MEarnhardt, JNLaipis, PJSilverman, DNBiophys J 74:3182-922001224Pubmed2011Structure and catalysis by carbonic anhydrase II: role of active-site tryptophan 5Mikulski, RDomsic, JFLing, GTu, CRobbins, AHSilverman, DNMcKenna, RArch Biochem Biophys 516:97-10221282642Pubmed2011Intramolecular proton shuttle supports not only catalytic but also noncatalytic function of carbonic anhydrase IIBecker, HMKlier, MSchüler, CMcKenna, RDeitmer, JWProc Natl Acad Sci U S A 108:3071-68083199Pubmed1994Interactions of active-site residues and catalytic activity of human carbonic anhydrase IIITu, CChen, XRen, XLoGrasso, PVJewell, DALaipis, PJSilverman, DNJ Biol Chem 269:23002-6234739Pubmed1975Proton magnetic resonance studies of carbonic anhydrase. II. Group controlling catalytic activityPesando, JMBiochemistry 14:681-820349499Pubmed2010Identification of potent and selective human carbonic anhydrase VII (hCA VII) inhibitorsGitto, RAgnello, SFerro, SVullo, DSupuran, CTChimirri, AChemMedChem 5:823-64994926Pubmed1971The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and CKhalifah, RGJ Biol Chem 246:2561-73120192Pubmed1979Characterization of human carbonic anhydrase III from skeletal muscleCarter, NJeffery, SShiels, AEdwards, YTipler, THopkinson, DABiochem Genet 17:837-541554744Pubmed1992Buffer dependence of CO2 hydration catalyzed by human carbonic anhydrase IRen, XLindskog, SBiochim Biophys Acta 1120:81-620578724Pubmed2010Structural and kinetic study of the extended active site for proton transfer in human carbonic anhydrase IIDomsic, JFWilliams, WFisher, SZTu, CAgbandje-McKenna, MSilverman, DNMcKenna, RBiochemistry 49:6394-96819139Pubmed1982A 13C nuclear magnetic resonance study of CO2/HCO-3 exchange catalyzed by human carbonic anhydrase ISimonsson, IJonsson, BHLindskog, SEur J Biochem 129:165-96433979Pubmed1984Anion inhibition of CO2 hydration catalyzed by human carbonic anhydrase II. Mechanistic implicationsTibell, LForsman, CSimonsson, ILindskog, SBiochim Biophys Acta 789:302-108399223Pubmed1993Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase IIISilverman, DNTu, CChen, XTanhauser, SMKresge, AJLaipis, PJBiochemistry 32:10757-6217427958Pubmed2007Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase IIIElder, IFisher, ZLaipis, PJTu, CMcKenna, RSilverman, DNProteins 68:337-43

4.2.1.1

Carbonic anhydrase dehydrates bicarbonate (cytosol)

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.<br>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.

Authored: May, B, 2011-08-06Reviewed: Jassal, B, 2012-05-16Reviewed: Silverman, DN, 2012-05-16Edited: May, B, 2011-08-06

Reactome DB_ID: 111627

Reactome DB_ID: 70106

Reactome DB_ID: 113528

Reactome DB_ID: 29356

PHYSIOL-LEFT-TO-RIGHT

ACTIVATION

Converted from EntitySet in Reactome

Reactome DB_ID: 1475034

Reactome Database ID Release 751475022Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1475022ReactomeR-HSA-1475022

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-1475022.1

4.2.1.1

Carbonic anhydrase hydrates carbon dioxide (plasma membrane)

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.

Authored: May, B, 2011-08-06Reviewed: Jassal, B, 2012-05-16Reviewed: Silverman, DN, 2012-05-16Edited: May, B, 2011-08-06

Reactome DB_ID: 1237009

extracellular regionGO0005576

Reactome DB_ID: 109276

Reactome DB_ID: 351626

Reactome DB_ID: 425425

PHYSIOL-LEFT-TO-RIGHT

ACTIVATION

Converted from EntitySet in Reactome

Reactome DB_ID: 1475027

plasma membraneGO0005886

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

Reactome Database ID Release 751475013Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1475013Reactome Database ID Release 751475025Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1475025ReactomeR-HSA-1475025

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-1475025.115501038Pubmed2004Carbonic anhydrase inhibitors: inhibition of the membrane-bound human isozyme IV with anionsInnocenti, AFirnges, MAAntel, JWurl, MScozzafava, ASupuran, CTBioorg Med Chem Lett 14:5769-7311676494Pubmed2001The catalytic properties of human carbonic anhydrase IXWingo, TTu, CLaipis, PJSilverman, DNBiochem Biophys Res Commun 288:666-918294854Pubmed2008Carbonic anhydrase activators: activation of the human tumor-associated isozymes IX and XII with amino acids and aminesPastorekova, SVullo, DNishimori, IScozzafava, APastorek, JSupuran, CTBioorg Med Chem 16:3530-611121027Pubmed2000Purification and kinetic analysis of recombinant CA XII, a membrane carbonic anhydrase overexpressed in certain cancersUlmasov, BWaheed, AShah, GNGrubb, JHSly, William STu, CSilverman, DNProc Natl Acad Sci U S A 97:14212-718162396Pubmed2008Carbonic anhydrase inhibitors. Interaction of 2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide with 12 mammalian isoforms: kinetic and X-ray crystallographic studiesTemperini, CCecchi, ABoyle, NAScozzafava, ACabeza, JEWentworth P, JrBlackburn, GMSupuran, CTBioorg Med Chem Lett 18:999-10052111324Pubmed1990Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidneyZhu, XLSly, William SJ Biol Chem 265:8795-8019054574Pubmed1997Catalysis and inhibition of human carbonic anhydrase IVBaird TT, JrWaheed, AOkuyama, TSly, William SFierke, CABiochemistry 36:2669-7818703501Pubmed2008Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymesHilvo, MBaranauskiene, LSalzano, AMScaloni, AMatulis, DInnocenti, AScozzafava, AMonti, SMDi Fiore, ADe Simone, GLindfors, MJänis, JValjakka, JPastoreková, SPastorek, JKulomaa, MSNordlund, HRSupuran, CTParkkila, SJ Biol Chem 283:27799-8097625839Pubmed1995Carbonic anhydrase IV: role of removal of C-terminal domain in glycosylphosphatidylinositol anchoring and realization of enzyme activityOkuyama, TWaheed, AKusumoto, WZhu, XLSly, William SArch Biochem Biophys 320:315-2216006130Pubmed2005Carbonic anhydrase inhibitors: inhibition of the human transmembrane isozyme XIV with a library of aromatic/heterocyclic sulfonamidesOzensoy, ONishimori, IVullo, DPuccetti, LScozzafava, ASupuran, CTBioorg Med Chem 13:6089-93

4.2.1.1

Carbonic anhydrase dehydrates bicarbonate (plasma membrane)

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.<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.

Authored: May, B, 2011-08-06Reviewed: Jassal, B, 2012-05-16Reviewed: Silverman, DN, 2012-05-16Edited: May, B, 2011-08-06

Reactome DB_ID: 351626

Reactome DB_ID: 425425

Reactome DB_ID: 1237009

Reactome DB_ID: 109276

PHYSIOL-LEFT-TO-RIGHT

ACTIVATION

Converted from EntitySet in Reactome

Reactome DB_ID: 1475027

Reactome Database ID Release 751475017Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1475017ReactomeR-HSA-1475017

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-1475017.1

4.2.1.1

Carbonic anhydrase hydrates carbon dioxide (mitochondria)

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.

Authored: May, B, 2011-08-06Reviewed: Jassal, B, 2012-05-16Reviewed: Silverman, DN, 2012-05-16Edited: May, B, 2011-08-06

Reactome DB_ID: 113521

mitochondrial matrixGO0005759

Reactome DB_ID: 29376

Reactome DB_ID: 29896

Reactome DB_ID: 113529

PHYSIOL-LEFT-TO-RIGHT

ACTIVATION

Converted from EntitySet in Reactome

Reactome DB_ID: 1475016

CA5A,B:Zinc [mitochondrial matrix]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntity

Reactome Database ID Release 751475031Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1475031Reactome Database ID Release 751475032Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1475032ReactomeR-HSA-1475032

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-1475032.116302824Pubmed2005Carbonic anhydrase inhibitors. The mitochondrial isozyme VB as a new target for sulfonamide and sulfamate inhibitorsNishimori, IVullo, DInnocenti, AScozzafava, AMastrolorenzo, ASupuran, CTJ Med Chem 48:7860-614611844Pubmed2003Carbonic anhydrase inhibitors: inhibition of human and murine mitochondrial isozymes V with anionsFranchi, MVullo, DGallori, EAntel, JWurl, MScozzafava, ASupuran, CTBioorg Med Chem Lett 13:2857-618356065Pubmed1993Human mitochondrial carbonic anhydrase: cDNA cloning, expression, subcellular localization, and mapping to chromosome 16Nagao, YPlatero, JSWaheed, ASly, William SProc Natl Acad Sci U S A 90:7623-710409679Pubmed1999Human mitochondrial carbonic anhydrase VB. cDNA cloning, mRNA expression, subcellular localization, and mapping to chromosome xFujikawa-Adachi, KNishimori, ITaguchi, TOnishi, SJ Biol Chem 274:21228-3317761422Pubmed2007Carbonic anhydrase inhibitors: the inhibition profiles of the human mitochondrial isoforms VA and VB with anions are very differentNishimori, IInnocenti, AVullo, DScozzafava, ASupuran, CTBioorg Med Chem 15:6742-7

4.2.1.1

Carbonic anhydrase dehydrates bicarbonate (mitochondria)

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.

Authored: May, B, 2011-08-06Reviewed: Jassal, B, 2012-05-16Reviewed: Silverman, DN, 2012-05-16Edited: May, B, 2011-08-06

Reactome DB_ID: 29896

Reactome DB_ID: 113529

Reactome DB_ID: 113521

Reactome DB_ID: 29376

PHYSIOL-LEFT-TO-RIGHT

ACTIVATION

Converted from EntitySet in Reactome

Reactome DB_ID: 1475016

Reactome Database ID Release 751475028Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1475028ReactomeR-HSA-1475028

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-1475028.1

4.2.1.1

Carbonic Anhydrase VI hydrates carbon dioxide to bicarbonate and a proton

H2O + CO2 -> H+ + HCO3-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.

Authored: May, B, 2011-03-24Reviewed: Jassal, B, 2012-05-16Reviewed: Silverman, DN, 2012-05-16Edited: May, B, 2011-03-24

Reactome DB_ID: 1237009

Reactome DB_ID: 109276

Reactome DB_ID: 351626

Reactome DB_ID: 425425

PHYSIOL-LEFT-TO-RIGHT

ACTIVATION

Reactome DB_ID: 1237316

CA6:Zinc [extracellular region]

CA6:Zinc

Carbonic Anhydrase VI:Zinc

Reactome DB_ID: 158417

zinc(2+) [ChEBI:29105]

zinc(2+)

ChEBI29105

Reactome DB_ID: 1237016

UniProt:P23280 CA6

CA6

CA6FUNCTION Reversible hydration of carbon dioxide. Its role in saliva is unknown.ACTIVITY REGULATION Inhibited by coumarins, sulfonamide derivatives such as acetazolamide (AZA), saccharin and Foscarnet (phosphonoformate trisodium salt).TISSUE SPECIFICITY Major constituent of saliva.SIMILARITY Belongs to the alpha-carbonic anhydrase family.

Homo sapiens

NCBI Taxonomy9606UniProtP23280

Chain Coordinates

EQUAL

308

EQUAL

Reactome Database ID Release 751237316Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1237316ReactomeR-HSA-1237316

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-1237316.1Reactome Database ID Release 751237060Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1237060Reactome Database ID Release 751237045Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1237045ReactomeR-HSA-1237045

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-1237045.117499996Pubmed2007Carbonic anhydrase activators: the first activation study of the human secretory isoform VI with amino acids and aminesNishimori, IOnishi, SVullo, DInnocenti, AScozzafava, ASupuran, CTBioorg Med Chem 15:5351-717228881Pubmed2007Carbonic anhydrase inhibitors. DNA cloning, characterization, and inhibition studies of the human secretory isoform VI, a new target for sulfonamide and sulfamate inhibitorsNishimori, IMinakuchi, TOnishi, SVullo, DScozzafava, ASupuran, CTJ Med Chem 50:381-89784398Pubmed1998Gustin from human parotid saliva is carbonic anhydrase VIThatcher, BJDoherty, AEOrvisky, EMartin, BMHenkin, RIBiochem Biophys Res Commun 250:635-41

4.2.1.1

Carbonic anhydrase VI dehydrates bicarbonate to water and carbon dioxide

H+ + HCO3- -> H2O + CO2Carbonic 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.

Authored: May, B, 2011-03-24Reviewed: Jassal, B, 2012-05-16Reviewed: Silverman, DN, 2012-05-16Edited: May, B, 2011-03-24

Reactome DB_ID: 351626

Reactome DB_ID: 425425

Reactome DB_ID: 1237009

Reactome DB_ID: 109276

PHYSIOL-LEFT-TO-RIGHT

ACTIVATION

Reactome DB_ID: 1237316

Reactome Database ID Release 751237081Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1237081ReactomeR-HSA-1237081

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-1237081.1

Reactome Database ID Release 751475029Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=1475029ReactomeR-HSA-1475029

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-1475029.111875253Pubmed2001The cellular physiology of carbonic anhydrasesBreton, SJOP 2:159-6420541618Pubmed2010Perspectives on carbonic anhydraseGilmour, KMComp Biochem Physiol A Mol Integr Physiol 157:193-719879980Pubmed2010Evaluating the role of carbonic anhydrases in the transport of HCO3--related speciesBoron, WFBiochim Biophys Acta 1804:410-2116679072Pubmed2006The structure and function of carbonic anhydrase isozymes in the respiratory system of vertebratesEsbaugh, AJTufts, BLRespir Physiol Neurobiol 154:185-98GO0015701

GO biological process