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4.2.1.1: carbonic anhydrase

This is an abbreviated version!
For detailed information about carbonic anhydrase, go to the full flat file.

Word Map on EC 4.2.1.1

Reaction

H2CO3
=
CO2
 +
H2O

Synonyms

(CA) XIV, AaCA1, alkalistable alpha-carbonic anhydrase, alpha carbonic anhydrase, alpha class carbonic anhydrase, alpha-CA, alpha-carbonic anhydrase, alpha-carbonic anhydrase isozyme II, alpha-class carbonic anhydrase, alpha-type CA, alpha-type carbonic anhydrase, alphaCA, alphaCA1, Am CA, AmCA, anhydrase, ASCA, AtCA1, AtCA2, AtCAL1, AtCAL2, B13-CA, BCA II, bCA IV, BCAII, BCAIIGln253Cys, beta carbonic anhydrase, beta-CA, beta-carbonic anhydrase, beta-class carbonic anhydrase, betaCA, betaCA1, BhCA, bovine carbonic anhydrase II, bsCA I, bsCA II, CA, CA 1, CA 3, CA I, CA II, CA III, CA IV, CA IX, CA VA, CA VB, CA VI, CA VII, CA VIII, CA XII, CA XIII, CA XIV, Ca XV, CA-I, CA-II, CA-III, CA-IX, CA-VA, CA-VB, CA-VI, CA-VII, CA-XII, CA-XIV, CA1, CA14x, CA2, CA2 homolog, CA2-like, CA3, CA4, CA5A, CA6, CA9, CAA, CAA1, CAA2, Cab, cab-type beta-class carbonic anhydrase, cadmium carbonic anhydrase, CAH3, CAH7, CAH8, CAI, CAII, CAIII, CAIV, CAIX, Cam, CamH, CaN, Can2, canA, canB, CaNce103, carbonate anhydrase, Carbonate dehydratase, carbonate dehydratase I, carbonate dehydratase III, Carbonate dehydratase IX, Carbonate dehydratase VA, Carbonate dehydratase VB, Carbonate dehydratase VI, Carbonate dehydratase VII, Carbonate dehydratase XII, Carbonate dehydratase XIV, carbonate hydro-lyase, carbonate hydrolase, carbonate hydrolyase, carbonic acid anhydrase, carbonic anhydrase, carbonic anhydrase 1, carbonic anhydrase 14, carbonic anhydrase 2, carbonic anhydrase 3, carbonic anhydrase 5A, carbonic anhydrase 6, carbonic anhydrase 9, carbonic anhydrase cambialistic enzyme, carbonic anhydrase I, carbonic anhydrase I (CA I) Michigan 1, carbonic anhydrase II, carbonic anhydrase III, carbonic anhydrase isozyme I, carbonic anhydrase isozyme II, carbonic anhydrase isozyme III, carbonic anhydrase isozyme IV, carbonic anhydrase isozyme IX, carbonic anhydrase IV, carbonic anhydrase IX, carbonic anhydrase type III, carbonic anhydrase V, carbonic anhydrase VA, carbonic anhydrase VI, carbonic anhydrase VII, carbonic anhydrase XII, carbonic anhydrase XIII, carbonic anhydrase XIV, carbonic anhydrase XV, carbonic anhydrase-I, carbonic anhydrase-II, carbonic anhydrase-related protein, carbonic anhydrase-related protein VIII, carbonic dehydratase, carboxyanhydrase, CARP, CAS1, CAS2, CasCAc, CasCAg, CAV, CAVA, CAXII, CcaA, CcmM, CDCA1, chloroplast carbonic anhydrase, clCA, CmCA, CO2 hydrase, CO2 hydratase, CPB, CpsCA, CpsCAgamma, CrCAH3, CsoSCA, cynT, CynT2, cytoplasmic carbonic anhydrase, Dca, dCA I, dCA II, dCAII, DDCA, dehydratase, carbonate, delta carbonic anhydrase, delta-carbonic anhydrase, delta-class CA, diatom carbonic anhydrase, Dsp-aCAopt sp., dual domain-carbonic anhydrase, dual-domain carbonic anhydrase, DVU_1777, E84A MTCA, eCA, ECCA, erythrocyte carbonic anhydrase, eta-CA, eta-carbonic anhydrase, external carbonic anhydrase, extracellular carbonic anhydrase, FbiCA 1, fCA, gamma carbonic anhydrase 1, gamma carbonic anhydrase 2, gamma carbonic anhydrase-like 1, gamma carbonic anhydrase-like 2, gamma-CA, gamma-CA1, gamma-CA2, gamma-CAL1, gamma-CAL2, gamma-carbonic anhydrase, gamma-class carbonic anhydrase, gammaCA, H216N ATCA, H64A HCA II, HC II, HCA, hCA I, HCA II, hCA III, hCA IV, hCA IX, hCA VA, hCA VB, hCA VI, hCA VII, hCA XII, hCA XIV, hCA XIV catalytic domain, HCA-I, HCA-II, hCAII, HcCA3, HICA, HP1186, hpalphaCA, hpbetaCA, human carbonic anhydrase, human carbonic anhydrase I, human carbonic anhydrase II, human carbonic anhydrase III, human carbonic anhydrase isoenzyme I, human carbonic anhydrase isoenzyme II, human carbonic anhydrase IX, human carbonic anhydrase XII, human carbonic anhydrase XIV, Ice-CA, icfA, isozyme CA II, isozyme CA IV, LdcCA, luminal carbonic anhydrase, lwCA, mCA V, mCA XIII, Membrane antigen MN, mesohalophilic carbonic anhydrase, MG-CA, MgaCA, More, mtcA1, mtcA2, MtCam, MTCY373.03, Nce103, NcoCA, NGCA, NstCcmM209, OEC33 protein, P54/58N, pentraxin-CA VI, pentraxin-carbonic anhydrase, PERMA_1443, PF3D7_1140000, PfCAdom, PgiCA, PgiCAb, PGJ_00014320, PhaCAgamma, PhCamH, photosystem II-associated carbonic anhydrase, Pl-can, plant-type (beta-class) carbonic anhydrase, PMCA, pMW1, poly-[Hb-SOD-CAT-CA], polyhemoglobin-superoxide dismutase-catalase-carbonic anhydrase, PtCA1, RCC-associated antigen G250, Renal cell carcinoma-associated antigen G250, RT erythrocyte CA, Rv1248, Rv1284, Rv3273, Rv3588c, SABP3, Salivary carbonic anhydrase, SazCA, scCA, Secreted carbonic anhydrase, secretory carbonic anhydrase, secretory carbonic anhydrase VI, SspCA, STPCA, STPCA-2, SULAZ_0541, TacA, TCAb, TCAc, TcCA, Tcru, Tcr_1545, Theam_1576, tobacco salicylic acid-binding protein 3, Tumor antigen HOM-RCC-3.1.3, TWCA1, TweCA, VchCA

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.1 carbonic anhydrase

Engineering

Engineering on EC 4.2.1.1 - carbonic anhydrase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H216N
Q158A
-
site-directed variant
Y212F
-
site-directed variant
Q253C
-
engineered protein
H64A
-
shuttling mutant CAII-H64A shows lower catalytic activity compared to wild-type. Mutant displays catalytic activity in intact oocytes, also reduces the SNAT3-associated membrane conductance, when glutamine, but not when asparagine is the substrate
G41A
the mutant has kcat/Km values similar to wild-type enzyme, and exhibits a similar dramatic decrease in catalytic activity at pH values below pH 8.0, but HICA-G41A is serendipitously found to bind sulfate ion or bicarbonate ion near pairs of Glu50 and Arg64 residues located on the dimerization interface, 2 of 12 chains in the asymmetric unit bind bicarbonate ion exclusively at the dimerization interface, while the remaining 10 chains bind bicarbonate ion exclusively at the allosteric site
V47A
the mutant has kcat/Km values similar to wild-type enzyme, and exhibits a similar dramatic decrease in catalytic activity at pH values below pH 8.0, but HICA-V47A is serendipitously found to bind sulfate ion or bicarbonate ion near pairs of Glu50 and Arg64 residues located on the dimerization interface, bicarbonate ions simultaneously bind to both the dimerization interface and the allosteric sites
A23C/L203C/C206S
mutant retains high catalytic efficiency, and differential scanning calorimetry shows acid stability and thermal stability that is enhanced compared with native enzyme
A65L
-
site-specific mutagenesis, enhancement of activity with all substrates, about 5fold increase in activity with 4-nitrophenyl acetate
A65L/T200G
-
site-specific mutagenesis, 5fold increase in activity with 4-nitrophenylacetate
A65L/T200R
-
site-specific mutagenesis, 4fold increase in activity with 4-nitrophenylacetate
A65S
the mutation can cause variations in binding affinity of small molecule inhibitors
A65S/N67Q/E69T/I91L/F131V/K170E/L204A
site-directed mutagenesis, active site mutant
C183S/C188S
mutations at positions 183 and 188 are to enhance crystallization by removing oxidizable cysteine residues. The positions of residues 183 and 188 are solvent exposed on the side of the enzyme opposite to the active site. The mutations C183S and C188S do not affect catalysis
E117A
-
oligonucleotide-directed mutagenesis
E234P
site-directed mutagenesis, residue Glu234, which is positioned in a surface loop, is substituted with a proline residue. Thermal stability analysis of this variant indicates an enhanced melting temperature of about 3°C compared to the wild-type enzyme
F131C
-
site-directed mutant
F198L
site-specific mutagenesis, HCA III
F198L/C183S/C188S
the ratio of turnover-number to Km-value for hydration of CO2 of mutant enzyme F198L/C183S/C188S is 25fold higher than the ratio of wild-type enzyme and mutant enzyme C183S/C188S
G8D/K18E/N24D/K36D/V39D/V50D/R57D/N62D/Q74E/T85D/Q136E/K169E/N177D/N186E/Q220E/L238E/N252D/Q254E
site-directed mutagenesis, mutant M4, shows reduced activity but increased thermostability and halostability compared to wild-type enzyme. The successful redesign of a mesohalophile enzyme to an extremely halotolerant orthologue, that is, one that is active at 3M NaCl and above. Role of Na+ in stabilizing M4 structure, molecular dynamics simulations, overview
G8D/K36D/V50D/N62D/Q136E/L238E
site-directed mutagenesis, mutant M2, shows reduced activity but increased thermostability and halostability compared to wild-type enzyme
G8D/N24D/K36D/V39D/V50D/R57D/N62D/Q74E/Q136E/K169E/L238E/N252D
site-directed mutagenesis, mutant M3, shows reduced activity but increased thermostability compared to wild-type enzyme
H200T
-
complex effect on the catalytic and inhibitor-binding properties
H64R
-
site-directed mutagenesis
H67N
-
complex effect on the catalytic and inhibitor-binding properties
H67R
site-directed mutagenesis, single point mutation in a critical region of the active site
H94N
-
oligonucleotide-directed mutagenesis
H94Q
-
oligonucleotide-directed mutagenesis
I91C
-
site-directed mutant
K170A
-
site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II
K170D
-
site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II
K170E
-
site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II
K170H
-
site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II
K64H/F198L
site-specific mutagenesis, HCA III
K64H/R67H
site-specific mutagenesis, HCA III
K64H/R67N
mutant has enhanced proton transfer in catalysis compared with wild-type HCA III
L100H/L224S/L240P
kcat/Km (CO2) decreased compared to wild-type, T(M): 65°C compared to wild-type: 58°C, T (inactivation): 65°C compared to wild-type: 60°C
L100H/L224S/L240P/Y7F
kcat/Km (CO2) slightly decreased compared to wild-type, T(M): 61.1°C compared to wild-type: 58°C, T (inactivation): 65°C compared to wild-type: 60°C
L100H/L224S/L240P/Y7F/N62L
kcat/Km (CO2) decreased compared to wild-type, T(M): 58.1°C compared to wild-type: 58°C, T (inactivation): 60°C compared to wild-type: 60°C
L100H/L224S/L240P/Y7F/N62L/N67Q
kcat/Km (CO2) slightly decreased compared to wild-type, T(M): 59.2°C compared to wild-type: 58°C, T (inactivation): 60°C compared to wild-type: 60°C
L100H/L224S/L240P/Y7F/N67Q
kcat/Km (CO2) decreased compared to wild-type, T(M): 62.7°C compared to wild-type: 58°C, T (inactivation): 65°C compared to wild-type: 60°C
L198A
-
site-specific mutagenesis, 5fold decrease in activity with 4-nitrophenylacetate
L204S
-
affinity for sulfonamides/sulfamate inhibitor is moderately decreased compared to wild-type. kcat and Km (CO2) comparable to wild-type
N24D/V39D/R57D/Q74E/K169E/N252D
site-directed mutagenesis, mutant M3, shows reduced activity but increased thermostability and halostability compared to wild-type enzyme
N62A
the mutant shows a predominantly inward orientation of the side chain of His64
N62C
-
site-directed mutant
N62L
the mutant shows a predominantly inward orientation of the side chain of His64
N62T
the mutant shows both inward and outward orientation of the side chain of His64 like the wild type enzyme
N62V
the mutant shows a predominantly inward orientation of the side chain of His64
N67I
-
affinity for sulfonamides/sulfamate inhibitor is highly decreased compared to wild-type. kcat and Km (CO2) comparable to wild-type
N67Q
the mutation can cause variations in binding affinity of small molecule inhibitors
Q92A
-
oligonucleotide-directed mutagenesis
Q92V
-
affinity for sulfonamides/sulfamate inhibitor is decreased compared to wild-type. kcat and Km (CO2) comparable to wild-type
R67N
-
mutant of carbonic anhydrase III, pH-dependent behavior and enhanced CO2 hydration activity compared to the wild-type enzyme, no enhanced hydrolysis rate
T199A
-
oligonucleotide-directed mutagenesis
T200A
-
site-specific mutagenesis, enhancement of activity with all substrates, about 2fold increase in activity with 4-nitrophenyl acetate
T200D
-
site-specific mutagenesis, 93fold decrease in activity with 4-nitrophenylacetate
T200G
-
site-specific mutagenesis, 3fold increase in activity with 4-nitrophenyl acetate
T200H
-
site-specific mutagenesis, enhancement of activity with all substrates, 2fold increase in activity with 4-nitrophenyl acetate
T200I
-
site-specific mutagenesis, enhancement of activity with all substrates, 1.5fold increase in activity with 4-nitrophenyl acetate
T200K
-
site-specific mutagenesis, enhancement of activity with all substrates, 1.3fold increase in activity with 4-nitrophenyl acetate
T200N
-
site-specific mutagenesis, enhancement of activity with all substrates
T200R
-
site-specific mutagenesis, enhancement of activity with all substrates, 7fold increase in activity with 4-nitrophenyl acetate
T200S
-
site-specific mutagenesis, 3fold increase in activity with 4-nitrophenyl acetate, decrease in activity with all other substrates
T200V
-
site-specific mutagenesis, decrease in activity with all substrates
V121A
-
site-specific mutagenesis, 4fold decrease in activity with 4-nitrophenylacetate
V143A
V143G
-
site-specific mutagenesis, 6fold decrease in activity with 4-nitrophenylacetate
V143I
-
mutant shows 20fold decreased catalytic activity compared to wild-type
V143L
-
mutant shows 20fold decreased catalytic activity compared to wild-type
V143Y
-
inactive mutant
V207A
-
site-specific mutagenesis, 1.5fold decrease in activity with 4-nitrophenylacetate
V62H/H67N/H200T
-
complex effect on the catalytic and inhibitor-binding properties
V62N
-
complex effect on the catalytic and inhibitor-binding properties
V62N/H67N
-
complex effect on the catalytic and inhibitor-binding properties
W5A
-
HCA III site-specific mutant
W5C
-
site-directed mutant
W5F
-
HCA III site-specific mutant
W5L
-
HCA III site-specific mutant
Y7A
-
site-directed mutagenesis
Y7D
-
site-directed mutagenesis
Y7F/T200G
-
site-specific mutagenesis, 1.5fold increase in activity with 4-nitrophenylacetate
Y7F/T200R
-
site-specific mutagenesis, 7.5fold increase in activity with 4-nitrophenylacetate
Y7H/F198L
site-specific mutagenesis, HCA III
Y7H/H64A
site-specific mutagenesisHCA II
Y7H/K64H
site-specific mutagenesis, HCA III
Y7H/K64H/F198L
site-specific mutagenesis, HCA III
Y7I
-
site-directed mutagenesis, replacement of Tyr7 with Ile has no effect on the interconversion of bicarbonate and CO2, but enhances intramolecular proton transfer approximately twofold. No changes occur in the ordered solvent structure in the active-site cavity or in the conformation of the side chain of the proton shuttle His64, while the first 11 residues of the amino-terminal chain in Y7I HCA II assume an alternate conformation compared to the wild-type enzyme
Y7N
-
site-directed mutagenesis
Y7R
-
site-directed mutagenesis
Y7S
-
site-directed mutagenesis
Y7W
-
site-directed mutagenesis
C148S
-
the mutation eliminate potential problems with the oxidation of the single cysteine residue at position 148
E62A
-
site-directed mutagenesis, large decrease in kcat
E62A/E84A
-
site-directed mutagenesis, large decrease in kcat
E62C
-
site-directed mutagenesis, large decrease in kcat
E62D
-
site-directed mutagenesis, 3fold decrease in kcat
E62D/E84D
-
site-directed mutagenesis, large decrease in kcat
E62H
-
site-directed mutagenesis, large decrease in kcat
E62Q
-
site-directed mutagenesis, large decrease in kcat
E62T
-
site-directed mutagenesis, large decrease in kcat
E62Y
-
site-directed mutagenesis, large decrease in kcat
E84 A
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 C
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 D
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 H
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 K
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 Q
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 S
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 Y
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84A
-
proton shuttle replaced with a residue that does not transfer protons
E88A
-
site-directed mutagenesis, large decrease in kcat
E89A
-
site-directed mutagenesis, large decrease in kcat
R59A
site-directed mutagenesis
R59C
site-directed mutagenesis
R59E
site-directed mutagenesis
R59H
site-directed mutagenesis
R59K
site-directed mutagenesis
R59M
site-directed mutagenesis
R59Q
site-directed mutagenesis
W19A
kcat/km at pH 7.5 is 2.5fold lower than wild-type value, kcat/km at pH 8.8 is 2.2fold lower than wild-type value
W19F
kcat/km at pH 7.5 is 5fold lower than wild-type value, kcat/km at pH 8.8 is 5.2fold lower than wild-type value
W19N
kcat/km at pH 7.5 is 3.2fold lower than wild-type value, kcat/km at pH 8.8 is 2.4fold lower than wild-type value
Y200A
kcat/km at pH 7.5 is 3.5fold higher than wild-type value, kcat/km at pH 8.8 is 3.3fold higher than wild-type value
Y200F
kcat/km at pH 7.5 is 3.6fold higher than wild-type value, kcat/km at pH 8.8 is 2.5fold lower than wild-type value
Y200S
kcat/km at pH 7.5 is 3fold higher than wild-type value, kcat/km at pH 8.8 is 3.3fold higher than wild-type value
D34A
-
site-directed mutagenesis
D34A/R36A
-
site-directed mutagenesis
D34E
-
site-directed mutagenesis
R36A
-
site-directed mutagenesis
R36K
-
site-directed mutagenesis
E115Q
-
site-directed mutagenesis, results in increased activity
E92Q
-
site-directed mutagenesis, results in increased activity
F65A/Y131C
-
covalently modified at cysteine residues with 4-chloromethylimidazole, exhibits an up to 3fold enhancement of catalytic activity over that of wild-type
His64Ala
-
100fold lower activity compared to the wild type enzyme
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
R94H/E92Q
-
site-directed mutagenesis
R94H/E92Q/I121V
-
site-directed mutagenesis
R94H/E92Q/I121V/I143V/I200T
-
site-directed mutagenesis
R94H/E92Q/I143V/I200T
-
site-directed mutagenesis
R94H/E92Q/I200T
-
site-directed mutagenesis
Y64H
-
the values of kcat/Km are very similar to those for the wild type enzyme
Y64H/F65A
-
CAV variant, double mutation, transforms CAVeffectively into an anlogue of CAII, the prototypical carbonic anhydrase isozyme
H66A
-
higher sensitivity to inhibitor 6-ethoxy-2-benzo-thiazolesulfonamide
C160S
-
completely inactive
C223S
-
completely inactive
E204A
-
completely inactive
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
H169N
-
little change in hydration activity
H208A
-
site-directed mutagenesis, mutant is more easily inactivated by oxidation than the wild-type enzyme
H208A/C272A
-
site-directed mutagenesis
H209N
-
somewhat defective in catalytic activity, to varying degrees in different buffers, 44% of wild-type activity in imidazole buffer
additional information