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Enzyme Nomenclature
Information on EC 4.2.1.1 - carbonic anhydrase
for references in articles please use BRENDA:EC4.2.1.1
Word Map on EC 4.2.1.1
- 4.2.1.1
- acetazolamide
- bicarbonate
- sulfonamide
-
hydration
- hypoxia
- glaucoma
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intraocular
- acidosis
- epithelium
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ocular
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acidification
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hypoxia-inducible
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metalloenzyme
- tubule
- na+
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perfuse
-
acid-base
- duct
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nanomolar
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histochemical
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reabsorption
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diuretic
-
basolateral
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tumor-associated
- gill
- osteoclast
- calcification
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cotransporter
- rubisco
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hypercapnia
-
acuity
-
antiepileptic
-
beta-blockers
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hypotensive
-
microelectrodes
-
open-angle
- h+-atpase
- furosemide
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anticonvulsant
- alkalosis
-
glut-1
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hif-1alpha
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branchial
- amiloride
- hydrochlorothiazide
- bumetanide
- analysis
-
glaucomatous
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thiazide
- medicine
- pharmacology
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biomineralization
- environmental protection
- drug development
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ccrcc
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
4.2.1.1
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RECOMMENDED NAME
GeneOntology No.
carbonic anhydrase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
H2CO3 = CO2 + H2O
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-
-
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H2CO3 = CO2 + H2O
carbonic anhydrase III is limited in rate by a step occuring outside the actual interconversion of CO2 and HCO3- and involving a change in bonding to hydrogen exchangeable with solvent water
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H2CO3 = CO2 + H2O
zinc-hydroxide mechanism, rate-determining H+ transfer step in catalytic mechanism
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H2CO3 = CO2 + H2O
the rate limiting step in catalysis of bicarbonate dehydration by HCA II is an intramolecular proton transfer from His64 to the zinc-bound hydroxide
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H2CO3 = CO2 + H2O
reaction mechanism, model of the active site designed on the basis of the X-ray crystal structure, proposed for both metal ions similar reaction pathways consisting in the nucleophilic attack by the metal bound hydroxide to the carbon dioxide with bicarbonate formation, in a next internal rotation of this last fragment, and then in the formation of a species ready for the product removal, overview
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H2CO3 = CO2 + H2O
reaction mechanism, model of the active site designed on the basis of the X-ray crystal structure, proposed for both metal ions similar reaction pathways consisting in the nucleophilic attack by the metal bound hydroxide to the carbon dioxide with bicarbonate formation, in a next internal rotation of this last fragment, and then in the formation of a species ready for the product removal, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
addition
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-
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dehydration
elimination
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-
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hydration
dehydration
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dehydration
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hydration
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-
hydration
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
carbonic acid hydro-lyase (carbon-dioxide-forming)
The enzyme catalyses the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. It is widespread and found in archaea, bacteria, and eukaryotes. Three distinct classes exist, and appear to have evolved independently. Contains zinc.
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CAS REGISTRY NUMBER
COMMENTARY
9001-03-0
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 1330; two beta class isozymes bsCA I and bsCA II, gene BR1829
Q8FVP0
UniProt
six genes, cah-1, cah-2, cah-3, cah-4, cah-5, and cah-6, possibly encoding alpha class carbonic anhydrases
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i.e. WL-chicken, male and female chicken, isozyme CA-II; male and female chicken, isozyme CA-II
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two distinct kinds of isoenzymes: high activity carbonic anhydrase and low activity carbonic anhydrase
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no activity in Homo sapiens
carbonic anhydrase XV is not expressed in humans, non-processed pseudogene
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33538, 33539, 33547, 33559, 33569, 33570, 33588, 649244, 650282, 650363, 650579, 651303, 652630, 652634, 652635, 652639, 652722, 664670, 665852, 680579, 696423, 698379, 701985, 703554, 715948, 728948
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strain 1330; two beta class isozymes bsCA I and bsCA II, gene BR1829
Q8FVP0
UniProt
i.e. WL-chicken, male and female chicken, isozyme CA-II; male and female chicken, isozyme CA-II
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33536, 33541, 33547, 33556, 33557, 33573, 649577, 649907, 650062, 650063, 650139, 650271, 650282, 650522, 650526, 650548, 650579, 651052, 651575, 651596, 652546, 652630, 652631, 652634, 652636, 652638, 652639, 652722, 652744, 652754, 653643, 653657, 666748, 679413, 696613, 696635, 696737, 696955, 697525, 698192, 699227, 699234, 699426, 699957, 700140, 700410, 700971, 701131, 702470, 702518, 702571, 702654, 702679, 702687, 703005, 703159, 703554, 703558, 705064, 713954, 714203, 714439, 714441, 714467, 716412, 716685, 729102, 729224, 729384, 730266
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649234, 649724, 649927, 650048, 652310, 652737, 678267, 678660, 678676, 678681, 678696, 678712, 678737, 680764, 696230, 696308, 696634, 698458, 698827, 699461, 700632, 702339, 702367, 702563, 705064, 705068, 713951, 728868, 730860
SwissProt
wild-type carbonic anhydrase I and active-site mutants V62N, H67N, H200T, double-mutant V62N,H67N, and triple-mutant V62H,H67N,H200T. Wild-type carbonic anhydrase II and active site mutant enzymes N62V, N67H and T200H
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SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
HICA is a type II member of the beta-carbonic anhydrase family
evolution
Q8FVP0
evolutionary tree of some bacterial beta-CAs among which the two Brucella suis isozymes bsCA I and bsCA II, phylogenetic analysis, overview
evolution
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phylogenetic analysis of beta-class carbonic anhydrases in invertebrates, overview
evolution
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carbonic anhydrase represents one of the most ancient proteins
evolution
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carbonic anhydrase represents one of the most ancient proteins
evolution
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evolutionary tree of some bacterial beta-CAs among which the two Brucella suis isozymes bsCA I and bsCA II, phylogenetic analysis, overview
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malfunction
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isozyme CAIX expression and activity is associated with metabolic dysfunction in MDA-MB-231 cells
malfunction
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CA IV-/- mice show a 32.13% reduction in total carbonic anhydrase activity and reduced beat frequency compared to the wild-type
malfunction
enzyme complements Saccharomyces cerevisiae deletion mutant Nce103; enzyme complements Saccharomyces cerevisiae deletion mutant Nce103
malfunction
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analyses of a cpb deletion mutant shows that Cpb is strictly required for growth when cultured in semi-defined medium and an atmosphere without CO2. Growth of the mutant is the same as that of the parent wild-type strain when cultured in nutrient-rich media with or without CO2 in the atmosphere, although elimination of glucose results in decreased production of acetate, propionate, and butyrate
malfunction
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at very low CO2 concentrations enzyme inhibition reduces photosynthesis
malfunction
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at very low CO2 concentrations eCA inhibition reduces photosynthesis
malfunction
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CA IV-/- mice show a 32.13% reduction in total carbonic anhydrase activity and reduced beat frequency compared to the wild-type
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physiological function
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isoform CA IX is involved in tumorigenesis through many pathways, such as pH regulation and cell adhesion control
physiological function
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beta carbonic anhydrase is required for scavenging CO2 from the ambient air
physiological function
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the enzyme from chicken has an important role in eggshell formation
physiological function
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CAIX is a zinc metalloenzyme that catalyzes the reversible hydration of CO2. CAIX expression is strongly induced by hypoxia and is significantly associated with tumor grade and poor survival
physiological function
isozyme LjCAA1 is involved in nitrogen ficxation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation; isozyme LjCAA2 is involved in nitrogen fixation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation
physiological function
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isoyzme CAII is associated with the acute mountain sickness, a common disease at high altitude
physiological function
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role of isozyme carbonic anhydrase IV in the bicarbonate-mediated activation of sperm, overview. Sperm respond to CO2 with an increase in beat frequency, an effect that can be inhibited by ethoxyzolamide. CA IV supplies sperm with HCO3-, which is necessary for stimulation of atypical sperm adenylyl cyclase and hence early activation of spermatozoa
physiological function
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role of isozyme carbonic anhydrase IV in the bicarbonate-mediated activation of sperm, overview. Sperm respond to CO2 with an increase in beat frequency, an effect that can be inhibited by ethoxyzolamide. CA IV supplies sperm with HCO3-, which is necessary for stimulation of atypical sperm adenylyl cyclase and hence early activation of spermatozoa
physiological function
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carbonic anhydrase which displays significant catalytic activity in intact oocytes, also reduces the SNAT3-associated membrane conductance, when glutamine, but not when asparagine is the substrate
physiological function
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a theoretical model predicts that homogeneous cytoplasmic distribution of CAII is more favourable for cellular transport of HCO3- and CO2 than is association of CAII with the cytoplasmic surface of the plasma membrane. Physiological interference with anion exchanger AE1 could not be demonstrated
physiological function
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beta carbonic anhydrase is required for scavenging CO2 from the ambient air
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physiological function
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the enzyme from chicken has an important role in eggshell formation
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physiological function
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isozyme LjCAA1 is involved in nitrogen ficxation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation; isozyme LjCAA2 is involved in nitrogen fixation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation
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physiological function
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role of isozyme carbonic anhydrase IV in the bicarbonate-mediated activation of sperm, overview. Sperm respond to CO2 with an increase in beat frequency, an effect that can be inhibited by ethoxyzolamide. CA IV supplies sperm with HCO3-, which is necessary for stimulation of atypical sperm adenylyl cyclase and hence early activation of spermatozoa
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additional information
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EGF induces CAIX translocation to lipid rafts but not its phosphorylation
additional information
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the wide use of dithiocarbamate pesticides may be one of the factors enhancing the vulnerability of this sturgeon species to pollutants, since they act as effective carbonate dehydratase inhibitors
additional information
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evaluation of efficiency of enzymes from Pseudomonas fragi, Micrococcus lylae, and Micrococcus luteus 2 compared to commercial Bos taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, the compared parameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous carbonic anhydrases and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine carbonic anhydrase
additional information
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evaluation of efficiency of enzymes from Pseudomonas fragi, Micrococcus lylae, and Micrococcus luteus 2 compared to commercial Bos taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, the compared parameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous carbonic anhydrases and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine carbonic anhydrase
additional information
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Pseudomonas fragi, Micrococcus lylae and Micrococcus luteus 2 along with a comparative evaluation of their efficiency compared to commercial Bis taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, aparameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous CAs and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine CA
additional information
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Pseudomonas fragi, Micrococcus lylae and Micrococcus luteus 2 along with a comparative evaluation of their efficiency compared to commercial Bis taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, aparameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous CAs and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine CA
additional information
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evaluation of efficiency of enzymes from Pseudomonas fragi, Micrococcus lylae, and Micrococcus luteus 2 compared to commercial Bos taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, the compared parameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous carbonic anhydrases and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine carbonic anhydrase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl acetate + H2O
2-nitrophenol + acetate
Helicobacter pylori ATCC 700392 / 26695 ATCC 700392 / 26695
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r
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
Helicobacter pylori ATCC 700392 / 26695 ATCC 700392 / 26695
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r
CO2 + H2O
H2CO3
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periplasmic alpha-carbonic anhydrase activity of Helicobacter pylori is essential for acid acclimation
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?
CO2 + H2O
H2CO3
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696230, 696308, 696613, 696634, 696737, 696955, 697525, 698458, 698469, 698814, 698827, 699227, 699246, 699426, 699461, 699957, 700140, 700410, 700632, 700971, 701131, 702339, 702367, 702470, 702518, 702563, 702571, 702654, 702679, 702687, 703005, 703159, 703554, 703558, 705064, 705068, 706515
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r
CO2 + H2O
H2CO3
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among the seven known isozymes carbonic anhydrase III is the least efficient in catalytic hydration of CO2
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r
CO2 + H2O
H2CO3
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roles for residues 7, 62, and 67 in finetuning the properties of His64 for optimal proton transfer in catalysis
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?
CO2 + H2O
H2CO3
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kinetics of SspCA is characterized in terms of first order CO2 hydration rate according to a procedure based on CO2 absorption tests in a stirred cell apparatus
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?
CO2 + H2O
H2CO3
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kinetics of SspCA is characterized in terms of first order CO2 hydration rate according to a procedure based on CO2 absorption tests in a stirred cell apparatus
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?
H2CO3
CO2 + H2O
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plays a role in various physiological functions, including interconversion between CO2 and HCO3- in intermediary metabolism, facilitated diffusion of CO2, pH homeostasis and ion transport
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r
H2CO3
CO2 + H2O