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Information on EC 4.2.1.1 - carbonic anhydrase and Organism(s) Mus musculus and UniProt Accession Q9D6N1
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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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Word Map
- 4.2.1.1
- acetazolamide
- bicarbonate
- sulfonamide
- isozymes
- hypoxia
- glaucoma
-
intraocular
- acidosis
- epithelium
-
hypoxia-inducible
-
metalloenzyme
- endothelial
-
ocular
-
acidification
-
acid-base
- na+
- tubule
- duct
-
tumor-associated
- prostaglandin
-
diuretic
- osteoclast
-
basolateral
- gill
- rubisco
- calcification
- topiramate
-
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: Mus musculus
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 XV
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 anhydrase XV
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 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
additional information
?
-
the enzyme is involved in various physiological processess such as acid-base balance and transport of CO2 and ions
-
-
?
additional information
?
-
-
the enzyme is involved in various physiological processess such as acid-base balance and transport of CO2 and ions
-
-
?
additional information
?
-
-
carbonic anhydrase IV mediates buffering in the extracellular space in central nervous system
-
-
?
additional information
?
-
-
carbonic anhydrase XIV may facilitate CO2 removal from neural retina and modulate photoreceptor function
-
-
?
additional information
?
-
-
carbonic anhydrase XIV mediates buffering in the extracellular space in central nervous system
-
-
?
additional information
?
-
the renal carbonic anhydrase type III plays a role in proximal tubule dysfunction
-
-
?
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
?
-
the enzyme is involved in various physiological processess such as acid-base balance and transport of CO2 and ions
-
-
?
additional information
?
-
-
the enzyme is involved in various physiological processess such as acid-base balance and transport of CO2 and ions
-
-
?
additional information
?
-
-
carbonic anhydrase IV mediates buffering in the extracellular space in central nervous system
-
-
?
additional information
?
-
-
carbonic anhydrase XIV may facilitate CO2 removal from neural retina and modulate photoreceptor function
-
-
?
additional information
?
-
-
carbonic anhydrase XIV mediates buffering in the extracellular space in central nervous system
-
-
?
additional information
?
-
the renal carbonic anhydrase type III plays a role in proximal tubule dysfunction
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme mCA XIII
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme mCA XIII
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme mCA XIII
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme mCA XIII
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
lack of proximal tubule CIC-5 is associated with CAIII induction
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
450000
CO2
-
truncated form of carbonic anhydrase VII lacking the amino-terminal 23 residues of recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002633
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme mCA XIII
0.00002
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme mCA XIII
0.000023
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme mCA XIII, i.e. daranide
0.000018
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme mCA XIII
0.00002
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme mCA XIII
0.000019
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme mCA XIII
0.000926
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
at 20°C and pH 7.5
0.000049
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
at 20°C and pH 7.5
0.000063
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
at 20°C and pH 7.5
0.000067
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
at 20°C and pH 7.5
0.00006
5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
at 20°C and pH 7.5
0.000049
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
at 20°C and pH 7.5
0.000048
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
at 20°C and pH 7.5
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00049
acetazolamide
Mus musculus
-
isoform carbonic anhydrase XIII, using 4-nitrophenyl acetate as substrate, at pH 7.4 and 25°C
0.00105
acetazolamide
Mus musculus
-
isoform carbonic anhydrase XIII, using 4-nitrophenyl phosphate as substrate, at pH 7.4 and 25°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
expressed in cortical and medullary ducts, carbonic anhydrase XIII
strongest expression of CA XIV is detected in the cortex region, where it is restricted to the proximal tubules of S1 and S2 segments, carbonic anhydrase XIV
CA XIV is highly expressed on both the basal and apical surfaces of the pigmented epithelial cells of the retina, carbonic anhydrase XIV
tibial anterior musle and soleus muscle, broad expression of CAIII in mouse skeletal muscles. Postnatal downregulation and reexpression of CAIII in adult tibial anterior muscle
additional information
immunohistochemic analysis using monoclonal antibody against CP3, mAb CP3, detailed overview. No CAIII is detected by CP3 in mouse heart and bladder smooth muscle, or in extensor digitorum longus muscle
additional information
-
immunohistochemic analysis using monoclonal antibody against CP3, mAb CP3, detailed overview. No CAIII is detected by CP3 in mouse heart and bladder smooth muscle, or in extensor digitorum longus muscle
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
murine sperm possesses extracellular isozyme CA IV that is transferred to the sperm surface as the sperm pass through the epididymis, the transfer takes place in the corpus epididymidis
-
murine sperm possesses extracellular isozyme CA IV that is transferred to the sperm surface as the sperm pass through the epididymis, the transfer takes place in the corpus epididymidis
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
CA IV-/- mice show a 32.13% reduction in total carbonic anhydrase activity and reduced beat frequency compared to the wild-type
malfunction
loss of CAIII in soleus and tibialanterior (TA) muscles in Car3-KO mice does not change muscle mass, sarcomere protein isoform contents, mitochondrial function, and the baseline twitch and tetanic contractility as compared with age-matched wild-type controls. Car3-KO TA muscle shows faster force reduction at the beginning but higher resistance at the end during a fatigue test, followed by slower postfatigue recovery than that of wild-type TA muscle. Superfused Car3-KO soleus muscle also have faster total force reduction during fatigue test than that of wild-type soleus. It shows less elevation of resting tension followed by a better postfatigue recovery under acidotic stress. Car3-KO increases the resistance of soleus muscle to acidosis
physiological function
-
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
expressing similar fast type of myofilament proteins, CAIII-positive tibial anterior muscle exhibits higher tolerance to fatigue than that of CAIII-negative fast twitch extensor digitorum longus muscle in in situ contractility studies
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). CAH13_MOUSE
262
0
29522
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
in SDS-PAGE the enzyme migrates as a 66000 Da disulfide-linked dimer, which turnes into a 31000 Da monomer upon reduction with DTT
additional information
-
in SDS-PAGE the enzyme migrates as a 66000 Da disulfide-linked dimer, which turnes into a 31000 Da monomer upon reduction with DTT
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized by hanging drop vapor diffusion method, crystals belong to space group P2(1) with unit cell dimesions a : 59.0 A, b : 75.6 A, c : 73.2 A
-
crystallized by the vapor diffusion method, hanging drop, space group C2, unit cell parameters a : 99.3 A, b : 66.7 A, c : 92.6 A
-
structure of the extracellular domain of murine CA XIV solved at 2.8 A resolution, and the enzyme-acetazolamide complex at 2.9 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F65A/Y131C
-
covalently modified at cysteine residues with 4-chloromethylimidazole, exhibits an up to 3fold enhancement of catalytic activity over that of wild-type
R117H
-
site-directed mutagenesis, replacement reconstructs a zinc-binding site and changes a catalytically inactive murine carbonic anhydrase-related protein to an active carbonic anhydrase
R94H
-
site-directed mutagenesis, replacement reconstructs a zinc-binding site and changes a catalytically inactive murine carbonic anhydrase-related protein to an active carbonic anhydrase
Y64H/F65A
-
CAV variant, double mutation, transforms CAVeffectively into an anlogue of CAII, the prototypical carbonic anhydrase isozyme
additional information
additional information
generation of Car3-knockout mice. Loss of CAIII in soleus and tibialanterior (TA) muscles in Car3-KO mice does not change muscle mass, sarcomere protein isoform contents, and the baseline twitch and tetanic contractility as compared with age-matched wild-type controls. Car3-KO TA muscle shows faster force reduction at the beginning but higher resistance at the end during a fatigue test, followed by slower postfatigue recovery than that of wild-type TA muscle. Superfused Car3-KO soleus muscle also have faster total force reduction during fatigue test than that of wild-type soleus. It shows less elevation of resting tension followed by a better postfatigue recovery under acidotic stress
additional information
-
generation of Car3-knockout mice. Loss of CAIII in soleus and tibialanterior (TA) muscles in Car3-KO mice does not change muscle mass, sarcomere protein isoform contents, and the baseline twitch and tetanic contractility as compared with age-matched wild-type controls. Car3-KO TA muscle shows faster force reduction at the beginning but higher resistance at the end during a fatigue test, followed by slower postfatigue recovery than that of wild-type TA muscle. Superfused Car3-KO soleus muscle also have faster total force reduction during fatigue test than that of wild-type soleus. It shows less elevation of resting tension followed by a better postfatigue recovery under acidotic stress
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mori, K.; Ogawa, Y.; Ebihara, K.; Tamura, N.; Tashiro, K.; Kuwahara, T.; Mukoyama, M.; Sugawara, A.; Ozaki, S.; Tanaka, I.; Nakao, K.
Isolation and characterization of CA XIV, a novel membrane-bound carbonic anhydrase from mouse kidney
J. Biol. Chem.
274
15701-15705
1999
Mus musculus (Q9WVT6), Mus musculus
Heck, R.W.; Tanhauser, S.M.; Manda, R.; Tu, C.; Laipis, P.J.; Silverman, D.N.
Catalytic properties of mouse carbonic anhydrase V
J. Biol. Chem.
269
24742-24746
1994
Mus musculus
Earnhardt, J.N.; Qian, M.; Tu, C.; Lakkis, M.M.; Bergenhem, N.C.H.; Laipis, P.J.; Tashian, R.E.; Silverman, D.N.
The catalytic properties of murine carbonic anhydrase VII
Biochemistry
37
10837-10845
1998
Mus musculus
Hurt, J.D.; Tu, C.; Laipis, P.J.; Silverman, D.N.
Catalytic properties of murine carbonic anhydrase IV
J. Biol. Chem.
272
13512-13518
1997
Mus musculus
Jude, K.M.; Wright, S.K.; Tu, C.; Silverman, D.N.; Viola, R.E.; Christianson, D.W.
Crystal structure of F65/Y131C-methylimidazole carbonic anhydrase V reveals architectural features of an engineered proton shuttle
Biochemistry
41
2485-2491
2002
Mus musculus
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
Elleby, B.; Sjoeblom, B.; Tu, C.; Silverman, D.N.; Lindskog, S.
Enhancement of catalytic efficiency by the combination of site-specific mutations in a carbonic anhydrase-related protein
Eur. J. Biochem.
267
5908-5915
2000
Mus musculus
Lehtonen, J.; Shen, B.; Vihinen, M.; Casini, A.; Scozzafava, A.; Supuran, C.T.; Parkkila, A.K.; Saarnio, J.; Kivelae, A.J.; Waheed, A.; Sly, W.S.; Parkkila, S.
Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family
J. Biol. Chem.
279
2719-2727
2004
Homo sapiens, Mus musculus (Q9D6N1), Mus musculus
Whittington, D.A.; Grubb, J.H.; Waheed, A.; Shah, G.N.; Sly, W.S.; Christianson, D.W.
Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV
J. Biol. Chem.
279
7223-7228
2004
Mus musculus
Hilvo, M.; Tolvanen, M.; Clark, A.; Shen, B.; Shah, G.N.; Waheed, A.; Halmi, P.; Hanninen, M.; Hamalainen, J.M.; Vihinen, M.; Sly, W.S.; Parkkila, S.
Characterization of CA XV, a new GPI-anchored form of carbonic anhydrase
Biochem. J.
392
83-92
2005
Pan troglodytes, Homo sapiens (P22748), Homo sapiens, Mus musculus (Q99N23), Mus musculus
Shah, G.N.; Ulmasov, B.; Waheed, A.; Becker, T.; Makani, S.; Svichar, N.; Chesler, M.; Sly, W.S.
Carbonic anhydrase IV and XIV knockout mice: roles of the respective carbonic anhydrases in buffering the extracellular space in brain
Proc. Natl. Acad. Sci. USA
102
16771-16776
2005
Mus musculus
Nagelhus, E.A.; Mathiisen, T.M.; Bateman, A.C.; Haug, F.M.; Ottersen, O.P.; Grubb, J.H.; Waheed, A.; Sly, W.S.
Carbonic anhydrase XIV is enriched in specific membrane domains of retinal pigment epithelium, Muller cells, and astrocytes
Proc. Natl. Acad. Sci. USA
102
8030-8035
2005
Mus musculus
Alterio, V.; De Simone, G.; Monti, S.M.; Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase inhibitors: inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides - solution and crystallographic studies
Bioorg. Med. Chem. Lett.
17
4201-4207
2007
Helicobacter pylori (O24855), Helicobacter pylori (Q1CVF1), Homo sapiens (O43570), Homo sapiens (P00915), Homo sapiens (P00918), Homo sapiens (P07451), Homo sapiens (P22748), Homo sapiens (P23280), Homo sapiens (P35218), Homo sapiens (P43166), Homo sapiens (Q16790), Homo sapiens (Q9ULX7), Homo sapiens (Q9Y2D0), Homo sapiens, Methanosarcina thermophila (P40881), Mus musculus (Q9D6N1)
Temperini, C.; Innocenti, A.; Mastrolorenzo, A.; Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and X-ray crystallographic studies
Bioorg. Med. Chem. Lett.
17
4866-4872
2007
Homo sapiens (P00915), Homo sapiens (P00918), Homo sapiens (P07451), Homo sapiens (P22748), Homo sapiens (P23280), Homo sapiens (P35218), Homo sapiens (P43166), Homo sapiens (Q16790), Homo sapiens (Q9ULX7), Homo sapiens (Q9Y2D0), Mus musculus (Q9D6N1)
Guezel, O.; Temperini, C.; Innocenti, A.; Scozzafava, A.; Salman, A.; Supuran, C.T.
Carbonic anhydrase inhibitors. Interaction of 2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide with 12 mammalian isoforms: kinetic and X-ray crystallographic studies
Bioorg. Med. Chem. Lett.
18
152-158
2008
Homo sapiens (O14939), Homo sapiens (P00915), Homo sapiens (P00918), Homo sapiens (P07451), Homo sapiens (P22748), Homo sapiens (P23280), Homo sapiens (P35218), Homo sapiens (P43166), Homo sapiens (Q16790), Homo sapiens (Q9ULX7), Homo sapiens (Q9Y2D0), Mus musculus (Q9D6N1)
Temperini, C.; Cecchi, A.; Boyle, N.A.; Scozzafava, A.; Cabeza, J.E.; Wentworth, P.; Blackburn, G.M.; Supuran, C.T.
Carbonic anhydrase inhibitors. Interaction of 2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide with 12 mammalian isoforms: Kinetic and X-ray crystallographic studies
Bioorg. Med. Chem. Lett.
18
999-1005
2007
Homo sapiens (O43570), Homo sapiens (P00915), Homo sapiens (P00918), Homo sapiens (P07451), Homo sapiens (P22748), Homo sapiens (P23280), Homo sapiens (P35218), Homo sapiens (P43166), Homo sapiens (Q16790), Homo sapiens (Q9ULX7), Homo sapiens (Q9Y2D0), Mus musculus (Q9D6N1)
Hilvo, M.; Supuran, C.T.; Parkkila, S.
Characterization and inhibition of the recently discovered carbonic anhydrase isoforms CA XIII, XIV and XV
Curr. Top. Med. Chem.
7
893-899
2007
Homo sapiens, Homo sapiens (Q9ULX7), Mus musculus, Mus musculus (Q9D6N1), no activity in Homo sapiens
Innocenti, A.; Scozzafava, A.; Parkkila, S.; Puccetti, L.; De Simone, G.; Supuran, C.T.
Investigations of the esterase, phosphatase, and sulfatase activities of the cytosolic mammalian carbonic anhydrase isoforms I, II, and XIII with 4-nitrophenyl esters as substrates
Bioorg. Med. Chem. Lett.
18
2267-2271
2008
Homo sapiens, Mus musculus
Innocenti, A.; Hilvo, M.; Scozzafava, A.; Parkkila, S.; Supuran, C.T.
Carbonic anhydrase inhibitors: Inhibition of the new membrane-associated isoform XV with phenols
Bioorg. Med. Chem. Lett.
18
3593-3596
2008
Mus musculus
Temperini, C.; Innocenti, A.; Scozzafava, A.; Supuran, C.T.
Carbonic anhydrase inhibitors. Interaction of the antitumor sulfamate EMD 486019 with twelve mammalian carbonic anhydrase isoforms: Kinetic and X-ray crystallographic studies
Bioorg. Med. Chem. Lett.
18
4282-4286
2008
Mus musculus, Homo sapiens (P00918)
Hilvo, M.; Innocenti, A.; Monti, S.M.; De Simone, G.; Supuran, C.T.; Parkkila, S.
Recent advances in research on the most novel carbonic anhydrases, CA XIII and XV
Curr. Pharm. Des.
14
672-678
2008
Homo sapiens, Mus musculus
Hilvo, M.; Salzano, A.M.; Innocenti, A.; Kulomaa, M.S.; Scozzafava, A.; Scaloni, A.; Parkkila, S.; Supuran, C.T.
Cloning, expression, post-Translational modifications and inhibition Studies on the latest mammalian carbonic anhydrase isoform, CA XV
J. Med. Chem.
52
646-654
2009
Mus musculus (Q99N23), Mus musculus
Gailly, P.; Jouret, F.; Martin, D.; Debaix, H.; Parreira, K.S.; Nishita, T.; Blanchard, A.; Antignac, C.; Willnow, T.E.; Courtoy, P.J.; Scheinman, S.J.; Christensen, E.I.; Devuyst, O.
A novel renal carbonic anhydrase type III plays a role in proximal tubule dysfunction
Kidney Int.
74
52-61
2008
Mus musculus (P16015)
Innocenti, A.; Hilvo, M.; Parkkila, S.; Scozzafava, A.; Supuran, C.
Carbonic anhydrase inhibitors: The membrane-associated isoform XV is highly inhibited by inorganic anions
Bioorg. Med. Chem. Lett.
19
1155-1158
2009
Mus musculus
Wandernoth, P.M.; Raubuch, M.; Mannowetz, N.; Becker, H.M.; Deitmer, J.W.; Sly, W.S.; Wennemuth, G.
Role of carbonic anhydrase IV in the bicarbonate-mediated activation of murine and human sperm
PLoS ONE
5
e15061
2010
Homo sapiens, Mus musculus, Mus musculus C57/BL6J
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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