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Information on EC 4.2.1.1 - carbonic anhydrase and Organism(s) Bos taurus and UniProt Accession P00921
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4.2.1.1 carbonic anhydraseIUBMB Comments
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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- 4.2.1.1
- acetazolamide
- bicarbonate
- sulfonamide
- isozymes
- hypoxia
- glaucoma
-
intraocular
- acidosis
- epithelium
-
hypoxia-inducible
-
metalloenzyme
- endothelial
-
ocular
-
acidification
-
acid-base
- na+
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-
tumor-associated
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-
diuretic
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-
basolateral
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-
reabsorption
-
cotransporter
-
electrolyte
-
glut-1
-
branchial
-
open-angle
-
antiepileptic
-
beta-blockers
- h+-atpase
-
acuity
- hif-1alpha
-
hypotensive
-
anticonvulsant
-
hypercapnia
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-
microelectrodes
- amiloride
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-
biomineralization
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- pharmacology
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- diagnostics
-
cystoid
-
thiazide
- medicine
- hydrochlorothiazide
- analysis
-
glaucomatous
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
carbonic anhydrase, ca ix, ca ii, hca ii, hca i, carbonic anhydrase ix, carbonic anhydrase ii, hca ix, ca iv, anhydrase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
anhydrase
-
-
-
-
CA
CA-IX
-
-
-
-
CA-VA
-
-
-
-
CA-VB
-
-
-
-
CA-VI
-
-
-
-
CA-VII
-
-
-
-
CA-XII
-
-
-
-
CA-XIV
-
-
-
-
CA1
-
-
-
-
CA2
-
-
-
-
CAIX
-
-
-
-
carbonate anhydrase
-
-
-
-
Carbonate dehydratase
-
-
-
-
Carbonate dehydratase IX
-
-
-
-
Carbonate dehydratase VA
-
-
-
-
Carbonate dehydratase VB
-
-
-
-
Carbonate dehydratase VI
-
-
-
-
Carbonate dehydratase VII
-
-
-
-
Carbonate dehydratase XII
-
-
-
-
Carbonate dehydratase XIV
-
-
-
-
carbonic acid anhydrase
-
-
-
-
carbonic anhydrase
carbonic dehydratase
-
-
-
-
carboxyanhydrase
-
-
-
-
dehydratase, carbonate
-
-
-
-
Membrane antigen MN
-
-
-
-
P54/58N
-
-
-
-
pMW1
-
-
-
-
RCC-associated antigen G250
-
-
-
-
Renal cell carcinoma-associated antigen G250
-
-
-
-
Salivary carbonic anhydrase
-
-
-
-
Secreted carbonic anhydrase
-
-
-
-
Tumor antigen HOM-RCC-3.1.3
-
-
-
-
CA
-
-
-
-
carbonic anhydrase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
addition
-
-
-
-
hydration
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY
9001-03-0
-
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
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
H2CO3
CO2 + H2O
-
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
-
r
additional information
?
-
enzyme activity assay with 4-nitrophenyl acetate as substrate using the enzyme's esterase activity
-
-
?
additional information
?
-
-
BCA II when incubated under mildly denaturing condition of GdnHCl concentration of 1.5 M and a pH of 3.5 (slightly below its isoelectric point), forms ordered aggregates that are characteristically distinct from amorphous aggregates
-
-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
BCA II when incubated under mildly denaturing condition of GdnHCl concentration of 1.5 M and a pH of 3.5 (slightly below its isoelectric point), forms ordered aggregates that are characteristically distinct from amorphous aggregates
-
-
?
H2CO3
CO2 + H2O
-
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
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zinc
-
the Zn2+ enzyme remains essentially fourcoordinate in all its forms, although alterations in the K-edge shape imply differences in coordination geometry
Zn2+
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
required, carbonic anhydrase is a metalloenzyme, that binds a single zinc atom in its active site using three histidine ligands. The enzyme binds zinc relatively strongly with an apparent stability constant (log(KF)) of approximately 11.4 at pH 7.0. Following de novo protein synthesis, apocarbonic anhydrase must acquire and insert the enzymatically necessary zinc atom into the active site. The enzyme accepts donation of a single zinc atom from zinc-saturated metallothioneins at rates and concentrations that supports in vivo zinc donation by metallothionein (MT), fully saturated Zn-MT is capable of donating zinc to the apoenzyme. Competitive zinc titration to a solution containing equal concentrations of apo-rhMT1A and apoCA, formation of the fully metalated Zn7MT and holo-ZnCA, kinetics, simulation and modelling, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1'-(tribromo-lambda5-stibanediyl)bis(2-aminopyridin-1-ium)
29.9% inhibition of CO2 hydration reaction after 30 min
1,1'-(tribromo-lambda5-stibanediyl)bis(2-aminopyrimidin-1-ium)
57.6% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-amino-4,6-dimethoxy-5-sulfanylpyrimidin-1-ium)
99.3% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-aminopyridin-1-ium)
49.2% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-aminopyrimidin-1-ium)
98.4% inhibition of CO2 hydration reaction after 30 min
12,12,12-tribromo-7-oxo-6,7a,8,9,10,12-hexahydro-7H-12lambda5-pyrrolo[1',2':1,7][1,3,5,2]triazastibepino[4,3-b][1,3]benzothiazol-13-ium
2-[[(5-chlorothiophen-2-yl)(hydroxy)methyl]amino]-1-(trichloro[2-[2-(5-chlorothiophen-2-yl)-2-oxoethyl]pyrimidin-1-ium-1-yl]-lambda5-stibanyl)pyrimidin-1-ium
18.7% inhibition of CO2 hydration reaction after 30 min
3-amino-1,1,1-tribromo-4,5-dihydro-1H-1lambda5-[1,3,5,2]triazastibinino[1,6-a]benzimidazol-10-ium
35% inhibition of CO2 hydration reaction after 30 min
5,5,5-tribromo-1,2,3,7,8,9,9a,11,16,17a-decahydro-5H-5lambda5-dipyrrolo[2,1-c:1',2'-f][1,4,6,9,5]benzotetraazastibacycloundecine-10,17-dione
83.9% inhibition of CO2 hydration reaction after 30 min
6,6,6-trichloro-11-oxo-8,9,10,10a,11,12-hexahydro-6H-6lambda5-pyrimido[1,2-c]pyrrolo[2,1-g][1,3,5,2]triazastibepin-5-ium
31.0% inhibition of CO2 hydration reaction after 30 min
6-chloro-6,6-dimethyl-12-oxo-6,8,9,10,11,11a,12,13-octahydro-6lambda5-pyrido[2,1-g]pyrimido[1,2-c][1,3,5,2]triazastibepin-5-ium
99.3% inhibition of CO2 hydration reaction after 30 min
dibenzyl N',N'''-(tribromo-lambda5-stibanediyl)biscarbamimidothioate
36.0% inhibition of CO2 hydration reaction after 30 min
dibenzyl N',N'''-(trichloro-lambda5-stibanediyl)biscarbamimidothioate
26.7% inhibition of CO2 hydration reaction after 30 min
N'',N'''-bis[(E)-(2-chloro-5-nitrophenyl)methylidene]carbonic dihydrazide
-
2-(2,2-dichloroacetylamino)-1,3,4-thiadiazole-5-sulfonamide
-
noncompetitive inhibition
2-(3-chloropropionylamino)-1,3,4-thiadiazole-5-sulfonamide
-
noncompetitive inhibition
2-(3-phenylpropionylamino)-1,3,4-thiadiazole-5-sulfonamide
-
noncompetitive inhibition
5-[cis-5-norbornene-endo-3-carboxy-2-carboxamido]-1,3,4-thiadiazole-2-sulfonamide
-
-
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonamide
-
-
12,12,12-tribromo-7-oxo-6,7a,8,9,10,12-hexahydro-7H-12lambda5-pyrrolo[1',2':1,7][1,3,5,2]triazastibepino[4,3-b][1,3]benzothiazol-13-ium
-
12,12,12-tribromo-7-oxo-6,7a,8,9,10,12-hexahydro-7H-12lambda5-pyrrolo[1',2':1,7][1,3,5,2]triazastibepino[4,3-b][1,3]benzothiazol-13-ium
92.3% inhibition of CO2 hydration reaction after 30 min
acetazolamide
-
100 mM, the firmly-membrane-associated activity is less sensitive to inhibition than the loosely-membrane associated enzyme
Cl-
-
100 mM, the firmly-membrane-associated activity is less sensitive to inhibition than the loosely-membrane associated enzyme
I-
-
100 mM, the firmly-membrane-associated activity is less sensitive to inhibition than the loosely-membrane associated enzyme
KSCN
-
uncompetitive inhibition of outer peripheral, cytosolic, inner peripheral and integral isoenzyme
NaN3
-
uncompetitive inhibition of outer peripheral, cytosolic, inner peripheral and integral isoenzyme
sulfanilamide
-
uncompetitive inhibition of outer peripheral, cytosolic, inner peripheral and integral isoenzyme
additional information
antimony(III) complexes inhibit alpha-carbonic anhydrase isozyme II from bovine erythrocytes. No inhibition by 5
-
additional information
carbohydrazones as another class of carbonic anhydrase inhibitors, synthesis, kinetics, and ligand docking studies, overview. Single crystal X-ray diffraction, structural coordinates of bovine carbonic anhydrase (PDB ID 1V9E) is used for docking of carbohydrazone compounds, three-dimensional structure analysis. No inhibition by N'',N'''-bis[(E)-(4-chlorophenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2-fluorophenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-phenylmethylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2-hydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(3-hydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(4-hydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2,3-dihydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2,5-dihydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(5-bromo-2-hydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2,4,6-trihydroxyphenyl)methylidene]carbonicdihydrazide, N'',N'''-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2-methoxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(3-methoxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(4-methoxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2-hydroxy-5-methoxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2-hydroxy-3-methoxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(3-ethoxy-2-hydroxyphenyl)methylidene]carbonic dihydrazide, and N'',N'''-bis[(E)-(3,4-dimethoxyphenyl)methylidene]carbonic dihydrazide
-
additional information
-
dianionic inhibitors depress the rate of H+ transfer during turnover by stabilizing the protonated from of Lys64
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
influence of pH-value and buffer composition on Km-value on native enzyme and on an activated derivative with modified thiol groups
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
influence of pH-value and buffer composition and the native enzyme and on an activated derivative with modified thiol groups
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
(2,4,6-triisopropylphenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0021
(3,5-dichloro-2-hydroxyphenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.002
(3-chloro-4-nitrophenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.001
3-[[(aminosulfonyl)amino]sulfonyl]benzoic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0009
4-[[(aminosulfonyl)amino]sulfonyl]benzoic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.01
N-(4-[(E)-[(aminosulfonyl)imino]methyl]phenyl)acetamide
-
pH 7.4, 25°C, isozyme bCA IV
0.002
N-(4-[[(aminosulfonyl)amino]sulfonyl]phenyl)acetamide
-
pH 7.4, 25°C, isozyme bCA IV
0.07
N-(aminosulfonyl)-1,1,1-trichloromethanesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.07
N-(aminosulfonyl)-1,1,1-trifluoromethanesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.04
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,4-nonafluorobutane-1-sulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.03
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.009
N-(aminosulfonyl)-1-(7,7-dimethylbicyclo[2.2.1]hept-1-yl)methanesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0018
N-(aminosulfonyl)-2,3,4,5,6-pentafluorobenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0035
N-(aminosulfonyl)-2,4,6-triisopropylbenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0039
N-(aminosulfonyl)-2,4,6-tripropylbenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0032
N-(aminosulfonyl)-2,5-dichlorobenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0021
N-(aminosulfonyl)-3,5-dichloro-2-hydroxybenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0026
N-(aminosulfonyl)-3-(trifluoromethyl)benzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.003
N-(aminosulfonyl)-3-chloro-4-nitrobenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.01
N-(aminosulfonyl)-5-(dimethylamino)naphthalene-1-sulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.000073
N-salicylidene-sulfanilic acid amide cobalt acetate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.000078
N-salicylidene-sulfanilic acid amide cobalt chloride complex
-
pH 7.4, 25°C, isozyme bCA IV
0.000073
N-salicylidene-sulfanilic acid amide cobalt nitrate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.000072
N-salicylidene-sulfanilic acid amide cobalt sulfate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.000083
N-salicylidene-sulfanilic acid amide copper chloride complex
-
pH 7.4, 25°C, isozyme bCA IV
0.00008
N-salicylidene-sulfanilic acid amide copper nitrate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.000108
N-salicylidene-sulfanilic acid amide nickel acetate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.000105
N-salicylidene-sulfanilic acid amide nickel chloride complex
-
pH 7.4, 25°C, isozyme bCA IV
0.000102
N-salicylidene-sulfanilic acid amide nickel nitrate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.000106
N-salicylidene-sulfanilic acid amide nickel sulfate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.01
N-[(1E)-(1-methyl-1H-pyrrol-2-yl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme bCA IV
0.01
N-[(1E)-(3,4,5-trimethoxyphenyl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme bCA IV
0.01
N-[(1E)-(5-methylthien-2-yl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme bCA IV
0.008
N-[(1E)-[4-(dimethylamino)phenyl]methylene]sulfamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0016
tert-butyl 3-[[(aminosulfonyl)amino]sulfonyl]phenylcarbamate
-
pH 7.4, 25°C, isozyme bCA IV
0.002
tert-butyl 4-[[(aminosulfonyl)amino]sulfonyl]phenylcarbamate
-
pH 7.4, 25°C, isozyme bCA IV
0.0024
tert-butyl 5-[[(aminosulfonyl)amino]sulfonyl]-2-hydroperoxyphenylcarbamate
-
pH 7.4, 25°C, isozyme bCA IV
0.006
[(7,7-dimethylbicyclo[2.2.1]hept-1-yl)methyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0015
[3-(trifluoromethyl)phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0012
[3-[(tert-butoxycarbonyl)amino]-4-hydroperoxyphenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.01
[3-[(tert-butoxycarbonyl)amino]phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0015
[4-(acetylamino)phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0012
[4-[(tert-butoxycarbonyl)amino]phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.008
[5-(dimethylamino)-1-naphthyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0003
[[(2-methylphenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0009
[[(2-methylphenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme bCA IV
0.0004
[[(4-chlorophenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0011
[[(4-chlorophenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme bCA IV
0.0003
[[(4-fluorophenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0012
[[(4-fluorophenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme bCA IV
0.0006
[[(4-methylphenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0014
[[(4-methylphenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme bCA IV
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
outer peripheral, inner peripheral or integral localization
-
-
association of the enzyme with light microsomal membranes is dependent on pH, being lower at neutral or alkaline pH. 2 Enzyme forms: a loosely-membrane-associated enzyme and a firmly-membrane-associated enzyme
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
additional information
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CAH2_BOVIN
260
0
29114
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
at least 20% carbohydrate, contains glucosamine, galactose and sialic acid
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals belong to hexagonal space group P6(1), with unit-cell parameters a : b : 66.7 A, c : 240.0 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
42%, 39% and 36% stability is observed at pH 8.0, pH 8.5, and pH 9.0, respectively for commercial bovine carbonic anhydrase following 6 h of incubation. After 3 h incubation at pH 7.0 and pH 7.5, bovin retains 81% and 75% residual activity, while 79%, 69%, 61%, stability is observed at pH 8.0, pH 8.5, and pH 9.0, respectively. Effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview
715948
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
the enzyme possesses two stable folded conformers with the conformational transition occurring at about 30°C. The methodology yields a stability curve for the complete unfolding of the enzyme below this temperature but only the partial unfolding, to the molten globule state, above it. The transition state thermodynamics for the low-term to physiological-temperature conformational change are calculated from slow-scan-rate differential scanning calorimetry measurements where it is found that the free energy barrier for the conversion is 90 kJ/mole and the transition state possesses a substantial unfolding quality
additional information
-
effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the enzyme from a commercial preparation is further purified by gel filtration and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
discovery and development of carbonic anhydrase inhibitors is crucial for their clinical use as antiepileptic, diurectic, and antiglaucoma agents
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
-
the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Engberg, P.; Millqvist, E.; Pohl, G.; Lindskog, S.
Purification and some properties of carbonic anhydrase from bovine skeletal muscle
Arch. Biochem. Biophys.
241
628-638
1985
Bos taurus
Henkens, R.W.; Kitchell, B.B.; Lottich, S.C.; Stein, P.J.; Williams, T.J.
Detection and characterization using circular dichroism and fluorescence spectroscopy of a stable intermediate conformation formed in the denaturation of bovine carbonic anhydrase with guanidinium chloride
Biochemistry
21
5918-5923
1982
Bos taurus
Whitney, P.L.; Briggle, T.V.
Membrane-associated carbonic anhydrase purified from bovine lung
J. Biol. Chem.
257
12056-12059
1982
Bos taurus
Carter, M.J.
Carbonic anhydrase: isoenzymes, properties, distribution, and functional significance
Biol. Rev.
47
465-513
1972
Bos taurus, Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Mammalia, Petroselinum crispum, Rattus norvegicus
Atkins, C.A.
Occurence and some properties of carbonic anhydrases from legume root nodules
Phytochemistry
13
93-98
1974
Bos taurus, Vicia faba, Glycine max, Medicago sativa, Lupinus sp., Melilotus sp., Phaseolus vulgaris, Pisum sativum, Trifolium repens, Vicia sativa
-
Yachandra, V.; Powers, L.; Spiro, T.G.
X-ray absorption spectra and the coordination number of Zn and Co carbonic anhydrase as a function of pH and inhibitor binding
J. Am. Chem. Soc.
105
6596-6604
1983
Bos taurus
-
Ren, X.; Jonsson, B.H.; Millqvist, E.; Lindskog, S.
A comparison of the kinetic properties of native bovine muscle carbonic anhydrase and an activated derivative with modified thiol groups
Biochim. Biophys. Acta
953
79-85
1988
Bos taurus
Rowlett, R.S.; Gargiulo III, N.J.; Santoli, F.A.; Jackson, J.M.; Corbett, A.H.
Activation and inhibition of bovine carbonic anhydrase III by dianions
J. Biol. Chem.
266
93s-941
1961
Bos taurus
-
Mananes, A.A.L.; Daleo, G.R.; Vega, F.V.
pH-dependent association of carbonic anhydrase (CA) with gastric light microsomal membranes isolated from bovine abomasum. Partial characterization of membrane-associated activity
Comp. Biochem. Physiol. B
105
175-182
1993
Bos taurus
Saito, R.; Sato, T.; Ikai, A.; Tanaka, N.
Structure of bovine carbonic anhydrase II at 1.95 A resolution
Acta Crystallogr. Sect. D
60
792-795
2004
Bos taurus
Arslan, O.
Inhibition of bovine carbonic anhydrase by new sulfonamide compounds
Biochemistry (Moscow)
66
982-983
2001
Bos taurus
Qian, M.; Earnhardt, J.N.; Wadhwa, N.R.; Tu, C.; Laipis, P.J.; Silverman, D.N.
Proton transfer to residues of basic pKa during catalysis by carbonic anhydrase
Biochim. Biophys. Acta
1434
1-5
1999
Bos taurus, Homo sapiens, Mus musculus
Sandor,M.; Riechel, A.; Kaplan, I.; Mathiowitz, E.
Effect of lecithin and MgCO3 as additives on the enzymatic activity of carbonic anhydrase encapsulated in poly(lactide-co-glycolide) (PLGA) microspheres
Biochim. Biophys. Acta
1570
63-74
2002
Bos taurus
Gao, J.; Wu, Q.; Carbeck, J.; Lei, Q.P.; Smith, R.D.; Whitesides, G.M.
Probing the energetics of dissociation of carbonic anhydrase-ligand complexes in the gas phase
Biophys. J.
76
3253-3260
1999
Bos taurus, Homo sapiens
Alam, M.T.; Yamada, T.; Carlsson, U.; Ikai, A.
The importance of being knotted: effects of the C-terminal knot structure on enzymatic and mechanical properties of bovine carbonic anhydrase II
FEBS Lett.
519
35-40
2002
Bos taurus
Briganti, F.; Tilli, S.; Mincione, G.; Mincione, F.; Menabuoni, L.; Supuran, C.T.
Carbonic anhydrase inhibitors. Metal complexes of 5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide with topical intraocular pressure lowering properties: The influence of metal ions upon the pharmacological activity
J. Enzyme Inhib.
15
185-200
2000
Bos taurus, Homo sapiens
Scozzafava, A.; Banciu, M.D.; Popescu, A.; Supuran, C.T.
Carbonic anhydrase inhibitors: Inhibition of isozymes I, II and IV by sulfamide and sulfamic acid derivatives
J. Enzyme Inhib.
15
443-453
2000
Bos taurus, Homo sapiens
Casini, A.; Minicione, F.; Ilies, M.A.; Menabuoni, L.; Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase inhibitors: Synthesis and inhibition against isozymes I, II and IV of topically acting antiglaucoma sulfonamides incorporating cis-5-norbornene-endo-3-carboxy-2-carbxamido moieties
J. Enzyme Inhib.
16
113-123
2001
Bos taurus
Ul-Hassan, M.; Scozzafava, A.; Chohan, Z.H.; Supuran, C.T.
Carbonic anhydrase inhibitors: Metal complexes of a sulfanilamide derived schiff base and their interaction with isozymes I, II and IV
J. Enzyme Inhib.
16
499-505
2001
Bos taurus, Homo sapiens
Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase and matrix metalloproteinase inhibitors: Sulfonylated amino acid hydroxamates with MMP inhibitory properties act as efficient inhibitors of CA isozymes I, II, and IV, and N-hydroxysulfonamides inhibit both these zinc enzymes
J. Med. Chem.
43
3677-3687
2000
Bos taurus, Homo sapiens
Haritos, V.S.; Dojchinov, G.
Carbonic anhydrase metabolism is a key factor in the toxicity of CO2 and COS but not CS2 toward the flour beetle Tribolium castaneum [Coleoptera: Tenebrionidae]
Comp. Biochem. Physiol. C
140
139-147
2005
Bos taurus, Tribolium castaneum
Demir, Y.; Nadaroglu, H.; Demir, N.
Purification and characterization of carbonic anhydrase from bovine stomach and effects of some known inhibitors on enzyme activity
J. Enzyme Inhib. Med. Chem.
20
75-80
2005
Bos taurus
Hollowell, H.N.; Younvanich, S.S.; McNevin, S.L.; Britt, B.M.
Thermodynamic analysis of the low- to physiological-temperature nondenaturational conformational change of bovine carbonic anhydrase
J. Biochem. Mol. Biol.
40
205-211
2007
Bos taurus
Rana, A.; Gupta, T.P.; Bansal, S.; Kundu, B.
Formation of amyloid fibrils by bovine carbonic anhydrase
Biochim. Biophys. Acta
1784
930-935
2008
Bos taurus
Sun, X.C.; Li, J.; Cui, M.; Bonanno, J.A.
Role of carbonic anhydrase IV in corneal endothelial HCO3- transport
Invest. Ophthalmol. Vis. Sci.
49
1048-1055
2008
Bos taurus
Tasgin, E.; Nadaroglu, H.; Demir, Y.; Demir, N.
Purification and properties of carbonic anhydrase from bone marrow
Asian J. Chem.
21
5117-5122
2009
Bos taurus
-
Benfodda, Z.; Guillen, F.; Romestand, B.; Dahmani, A.; Blancou, H.
Synthesis and investigation of inhibition effect of fluorinated sulfonamide derivatives on carbonic anhydrase
Eur. J. Med. Chem.
45
1225-1229
2010
Bos taurus, Homo sapiens
Sharma, A.; Bhattacharya, A.
Enhanced biomimetic sequestration of CO2 into CaCO3 using purified carbonic anhydrase from indigenous bacterial strains
J. Mol. Catal. B
67
122-128
2010
Bos taurus, Micrococcus luteus, Micrococcus lylae, Pseudomonas fragi, Micrococcus luteus 2
-
Iqbal, S.; Nisar-ur-Rahman, S.; Iqbal, J.
A capillary electrophoresis-based enzyme assay for kinetics and inhibition studies of carbonic anhydrase
Anal. Biochem.
444
16-21
2014
Bos taurus
Pinter, T.B.; Stillman, M.J.
Kinetics of zinc and cadmium exchanges between metallothionein and carbonic anhydrase
Biochemistry
54
6284-6293
2015
Bos taurus (P00921)
Iqbal, S.; Saleem, M.; Azim, M.K.; Taha, M.; Salar, U.; Khan, K.M.; Perveen, S.; Choudhary, M.I.
Carbohydrazones as new class of carbonic anhydrase inhibitors synthesis, kinetics, and ligand docking studies
Bioorg. Chem.
72
89-101
2017
Bos taurus (P00921)
Di Fiore, A.; Alterio, V.; Monti, S.M.; De Simone, G.; D'Ambrosio, K.
Thermostable carbonic anhydrases in biotechnological applications
Int. J. Mol. Sci.
16
15456-15480
2015
Methanosarcina thermophila, Sulfurihydrogenibium azorense, Citrobacter freundii (A0A0D7LLM5), Caminibacter mediatlanticus (A6DAW8), Sulfurihydrogenibium sp. YO3AOP1 (B2V8E3), Persephonella marina (C0QRB5), Methanothermobacter thermautotrophicus (D9PU79), Thermovibrio ammonificans (E8T502), Serratia sp. ISTD04 (K4N028), Pyrococcus horikoshii (O59257), Homo sapiens (P00918), Bos taurus (P00921), Desulfovibrio vulgaris (Q72B61), Caminibacter mediatlanticus TB-2 (A6DAW8), Desulfovibrio vulgaris Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303 (Q72B61), Persephonella marina DSM 14350 / EX-H1 (C0QRB5), Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg (D9PU79), Thermovibrio ammonificans DSM 15698 / JCM 12110 / HB-1 (E8T502)
Karacan, M.S.; Rodionova, M.V.; Tunc, T.; Venedik, K.B.; Mamas, S.; Shitov, A.V.; Zharmukhamedov, S.K.; Klimov, V.V.; Karacan, N.; Allakhverdiev, S.I.
Characterization of nineteen antimony(III) complexes as potent inhibitors of photosystem II, carbonic anhydrase, and glutathione reductase
Photosynth. Res.
130
167-182
2016
Bos taurus (P00921), Pisum sativum (P17067)
EXTERNAL LINKS (specific for EC-Number 4.2.1.1)
Transporter Classification Database (TCDB): 8.A.164.1.1, 2.A.53.3.12
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