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Information on EC 4.2.1.1 - carbonic anhydrase and Organism(s) Pisum sativum and UniProt Accession P17067
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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+
- 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: Pisum sativum
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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1'-(tribromo-lambda5-stibanediyl)bis(2-aminopyridin-1-ium)
31.6% inhibition of CO2 hydration reaction after 30 min
1,1'-(tribromo-lambda5-stibanediyl)bis(2-aminopyrimidin-1-ium)
16.3% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-amino-4,6-dimethoxy-5-sulfanylpyrimidin-1-ium)
64.8% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-aminopyridin-1-ium)
9.4% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-aminopyrimidin-1-ium)
90.2% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis[2-amino-4,6-dimethoxy-5-[(1H-tetrazol-5-yl)sulfanyl]pyrimidin-1-ium]
14.3% 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
62.5% inhibition of CO2 hydration reaction after 30 min
3-amino-1,1,1-trichloro-4,5-dihydro-1H-1lambda5-[1,3,5,2]triazastibinino[1,6-a]benzimidazol-10-ium
10.0% 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
9.9% 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
25.1% 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
22.9% inhibition of CO2 hydration reaction after 30 min
dibenzyl N',N'''-(trichloro-lambda5-stibanediyl)biscarbamimidothioate
54.4% inhibition of CO2 hydration reaction after 30 min
ethoxyzolamide
-
effectively suppresses the carbonic anhydrase activity of photosystem 2 membranes. Carbonic anhydrase activity of PS1 membranes is suppressed alike by both inhibitors
additional information
antimony(III) complexes inhibit glutathione reductase activity of chloroplast, and a number of them also exhibit good inhibitory efficiency against the photosynthetic and carbonic anhydrase activity of Pisum sativum photosystem II
-
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
11.1% 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
18.4% inhibition of CO2 hydration reaction after 30 min
acetazolamide
-
increases carbonic anhydrase activity of photosystem 2 membranes at concentrations lower than 0.001 mM and suppresses this activity only at higher concentrations. Carbonic anhydrase activity of photosystem 1 membranes is suppressed
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetazolamide
-
increases carbonic anhydrase activity of photosystem 2 membranes at concentrations lower than 0.001 mM and suppresses this activity only at higher concentrations. Carbonic anhydrase activity of photosystem 1 membranes is suppressed
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000001
ethoxyzolamide
Pisum sativum
-
carbonic anhydrase activity of photosystem 2 membranes
SPECIFIC ACTIVITY [µmol/min/mg]
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
-
membrane. Activity of photosystem 1 membranes if calculated on chlorophyll basis is much higher than the activity of photosystem 2 membranes
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). CAHC_PEA
328
0
35377
Swiss-Prot
Chloroplast (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
194000
-
gel filtration, meniscus depletion equilibrium sedimentation, analytical ultracentrifugation
25000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
precursor OEC33 has a MW of 41000 Da, mature enzyme has a MW of 33000 Da
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with the inhibitor acetic acid, crystals of the orthorhombic space group C222 with cell parameters a : 136.9 A, b : 143.3 A, c : 202.1 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E276A
-
somewhat defective in catalytic activity, to varying degrees in different buffers. 40% of wild-type activity in HEPES/KOH buffer, 77.5% of wild-type activity in imidazole buffer, 6% of wild-type activity in HEPES/KOH buffer
H208A
-
site-directed mutagenesis, mutant is more easily inactivated by oxidation than the wild-type enzyme
H209N
-
somewhat defective in catalytic activity, to varying degrees in different buffers, 44% of wild-type activity in imidazole buffer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Kisiel, W.; Graf, G.
Purification and characterization of carbonic anhydrase from Pisum sativum
Phytochemistry
11
113-117
1972
Pisum sativum
-
Provart, N.J.; Majeau, N.; Coleman, J.R.
Characterization of pea chloroplastic carbonic anhydrase. Expression in Escherichia coli and site-directed mutagenesis
Plant Mol. Biol.
22
937-943
1993
Pisum sativum
Bjoerkbacka, H.; Johansson, I.M.; Forsman, C.
Possible roles for His 208 in the active-site region of chloroplast carbonic anhydrase from Pisum sativum
Arch. Biochem. Biophys.
361
17-24
1999
Pisum sativum
Kimber, M.S.; Pai, E.F.
The active site architecture of Pisum sativum beta-carbonic anhydrase is a mirror image of that of alpha-carbonic anhydrases
EMBO J.
19
1407-1418
2000
Pisum sativum
Lu, Y.K.; Theg, S.M.; Stemler, A.J.
Carbonic anhydrase activity of the photosystem II OEC33 protein from pea
Plant Cell Physiol.
46
1944-1953
2005
Pisum sativum
Ignatova, L.K.; Rudenko, N.N.; Khristin, M.S.; Ivanov, B.N.
Heterogeneous origin of carbonic anhydrase activity of thylakoid membranes
Biochemistry
71
525-532
2006
Pisum sativum
Rudenko, N.N.; Ignatova, L.K.; Ivanov, B.N.
Multiple sources of carbonic anhydrase activity in pea thylakoids: soluble and membrane-bound forms
Photosynth. Res.
91
81-89
2007
Pisum sativum
Lazova, G.N.; Stemler, A.J.
A 160 kDa protein with carbonic anhydrase activity is complexed with rubisco on the outer surface of thylakoids
Cell Biol. Int.
32
646-653
2008
Pisum sativum
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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