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Information on EC 4.2.1.1 - carbonic anhydrase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P53615
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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
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-
intraocular
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hypoxia-inducible
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metalloenzyme
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acid-base
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tumor-associated
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-
diuretic
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basolateral
- gill
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-
reabsorption
-
cotransporter
-
electrolyte
-
glut-1
-
branchial
-
open-angle
-
antiepileptic
-
beta-blockers
- h+-atpase
-
acuity
- hif-1alpha
-
hypotensive
-
anticonvulsant
-
hypercapnia
- alkalosis
-
microelectrodes
- amiloride
- furosemide
-
biomineralization
- drug development
- pharmacology
- environmental protection
- diagnostics
-
cystoid
-
thiazide
- medicine
- hydrochlorothiazide
- analysis
-
glaucomatous
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
-
-
-
-
carbonic anhydrase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
addition
-
-
-
-
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
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
a zinc ion is coordinated by the three highly conserved residues Cys57, His112 and Cys115
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4,5-dichloro-benzene-1,3-disulfonamide
-
shows effective carbonic anhydrase inhibitory activity
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
-
benzolamide
-
shows effective carbonic anhydrase inhibitory activity
brinzolamide
-
shows effective carbonic anhydrase inhibitory activity
dorzolamide
-
shows effective carbonic anhydrase inhibitory activity
ethoxzolamide
-
shows effective carbonic anhydrase inhibitory activity
methazolamide
-
shows effective carbonic anhydrase inhibitory activity
acetazolamide
-
shows effective carbonic anhydrase inhibitory activity
additional information
-
bromide, iodide and sulfamide, are the best anion inhibitors, with Ki values of 0.0087-0.0108 mM. Benzenesulfonamides substituted in 2-, 4- and 3,4-positions with amino, alkyl, halogeno and hydroxyalkyl moieties have Ki values in the range of 0.000976-0.01845 mM. Better inhibition with Ki values in the range of 154-654 nM is observed for benzenesulfonamides incorporating aminoalkyl/carboxyalkyl moieties or halogenosulfanilamides, benzene-1,3-disulfonamides, simple heterocyclic sulfonamides and sulfanilyl-sulfonamides. The clinically used sulfonamides/sulfamates, e.g. acetazolamide, ethoxzolamide, methazolamide, dorzolamide, topiramate, celecoxib, generally show effective scCA inhibitory activity, with Ki values in the range of 82.6-133 nM, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
L-adrenaline and some piperazines incorporating aminoethyl moieties were the most effective scCA activators
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
940000
CO2
-
pH not specified in the publication, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
98000
CO2
-
pH not specified in the publication, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.78
bicarbonate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.33
bisulfite
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.0108
bromide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.76
Carbonate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.85
chloride
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
31.7
Cyanate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
16.8
cyanide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
2.85
fluoride
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.33
hydrogen sulfide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.0103
Iodide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.46
nitrate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.4
phenylarsonic acid
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
38.2
phenylboronic acid
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.33
sulfamate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.0087
sulfamide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.58
sulfate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
55.6
thiocyanate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.0000151
4-(2-amino-pyrimidin-4-yl)-benzenesulfonamide
-
pH not specified in the publication, temperature not specified in the publication
0.000082
acetazolamide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000151
2-[(aminooxy)sulfinyl]-5-(2-chlorophenyl)-1,3,4-thiadiazole
Saccharomyces cerevisiae
-
-
0.000154
4-amino-N-(2-[4-[(aminooxy)sulfinyl]phenyl]ethyl)benzenesulfonamide
Saccharomyces cerevisiae
-
-
0.000166
4-amino-N-[4-[(aminooxy)sulfinyl]benzyl]benzenesulfonamide
Saccharomyces cerevisiae
-
-
0.000124
4-amino-N-[5-[(aminooxy)sulfinyl]-1,3,4-thiadiazol-2-yl]benzenesulfonamide
Saccharomyces cerevisiae
-
-
0.00036
5-[(aminooxy)sulfinyl]-3-methyl-1,3,4-thiadiazol-2(3H)-imine
Saccharomyces cerevisiae
-
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Nce103 in complex with a substrate analog at 2.04 A resolution, hanging drop vapor diffusion method, using 20% (w/v) PEG4000, 0.1 M sodium citrate, pH 5.6, 0.1 M sodium acetate, 20% (v/v) ethylene glycol, at 16°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the truncated Nce103 without the sequence coding for the N-terminal 13 residues Nce103DELTAN13 shows almost the same activity as the full length Nce103, whereas the activity of the truncated Nce103 without the sequence coding for the N-terminal 50 residues Nce103DELTAN50 is completely abolished
additional information
-
the truncated Nce103 without the sequence coding for the N-terminal 13 residues Nce103DELTAN13 shows almost the same activity as the full length Nce103, whereas the activity of the truncated Nce103 without the sequence coding for the N-terminal 50 residues Nce103DELTAN50 is completely abolished
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column chromatography and Superdex 75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Isik, S.; Kockar, F.; Arslan, O.; Guler, O.O.; Innocenti, A.; Supuran, C.T.
Carbonic anhydrase inhibitors. Inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with anions
Bioorg. Med. Chem. Lett.
18
6327-6331
2008
Saccharomyces cerevisiae
Isik, S.; Kockar, F.; Aydin, M.; Arslan, O.; Guler, O.O.; Innocenti, A.; Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase inhibitors: inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with sulfonamides and sulfamates
Bioorg. Med. Chem.
17
1158-1163
2009
Saccharomyces cerevisiae
Teng, Y.B.; Jiang, Y.L.; He, Y.X.; He, W.W.; Lian, F.M.; Chen, Y.; Zhou, C.Z.
Structural insights into the substrate tunnel of Saccharomyces cerevisiae carbonic anhydrase Nce103
BMC Struct. Biol.
9
67
2009
Saccharomyces cerevisiae (P53615), Saccharomyces cerevisiae
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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