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380000 - 1070000
histamine
additional information
additional information
-
0.0000005
CO2
-
mutant V143A, pH 8.3, 25°C
0.0000007
CO2
-
mutant V143I, pH 8.3, 25°C
0.000001
CO2
-
wild-type, pH 8.3, 25°C
0.0000011
CO2
-
mutant V143L, pH 8.3, 25°C
0.0004
CO2
-
pH 7.5, 25°C, wild-type CA XII
0.000493
CO2
pH 7.5, 25°C, enzyme cultured with supplemental zinc
0.00061
CO2
-
pH 5.5-7.5, 25°C, Zn-Cam
0.00104
CO2
-
pH 5.5-7.5, 25°C, Co-Cam
0.0052
CO2
pH 7.5, 25°C, enzyme cultured with supplemental iron
0.012
CO2
-
pH 9.0, 25°C, mutant R94H
0.019
CO2
-
pH 9.0, 25°C, mutant R94H/E92Q/I143V
0.023
CO2
-
pH 9.0, 25°C, mutant R94H/E92Q
0.034
CO2
-
pH 9.0, 25°C, mutant R94H/E92Q/I121V
0.038
CO2
-
pH 9.0, 25°C, mutant R94H/E92Q/I143V/I200T
0.039
CO2
-
pH 9.0, 25°C, mutant R94H/E92Q/I121V/I143V/I200T
0.046
CO2
-
pH 9.0, 25°C, mutant R94H/E92Q/I200T
0.05
CO2
-
pH 6.2, 25°C, mutant H208A
0.135
CO2
-
pH 6.2, 25°C, wild-type
0.28
CO2
-
pH 7.3, 25°C, mutant H208A
0.31
CO2
-
pH 7.3, 25°C, wild-type
0.74
CO2
-
pH 8.8, 25°C, wild-type
1.36
CO2
-
pH 8.8, 25°C, mutant H208A
2 - 8
CO2
pH 7.5, 37°C, variant R59A, 100 mM urea
6.08
CO2
-
pH 8.8, 25°C, mutant H208A
6.08
CO2
-
pH 8.8, 25°C, wild-type
10
CO2
pH 7.5, 37°C, variant R59Q, without guanidine hydrochloride
12
CO2
pH 7.5, 37°C, variant R59A, 100 mM 1.3-diaminoguanidine, variant R59H plus 100 mM guanidine hydrochloride
13
CO2
pH 7.5, 37°C, variant R59M, without guanidine hydrochloride
24
CO2
-
pH 8.5, 25°C, mutant R36A, MOPS buffer
30
CO2
-
pH 8.5, 25°C, mutant R36A, imidazole buffer
42
CO2
pH 7.5, 37°C, variant R59H, without guanidine hydrochloride
46
CO2
-
pH 8.5, 25°C, mutant R36A
47
CO2
-
pH 7.5, 25°C, variant E62Y, 50 mM MOPS buffer
67
CO2
pH 7.5, 37°C, variant R59E, without guanidine hydrochloride
70
CO2
pH 7.5, 37°C, variant R59A
85
CO2
-
pH 6.28, MES buffer, carbonic anhydrase I mutant V62N,H67N,H200T
92
CO2
-
pH 8.5, 25°C, mutant R36K
110
CO2
pH 7.5, 37°C, variant R59A, 100 mM imidazole
117
CO2
-
pH 6.3, MES buffer, wild-type carbonic anhydrase I
150
CO2
-
pH 7.9, temperature not specified in the publication, the activities depended on culture conditions, ranging between 20/sec and 150/sec
159
CO2
pH 7.5, 37°C, variant R59M, 100 mM guanidine hydrochloride
160
CO2
pH 7.5, 37°C, variant R59A, 100 mM ethylamine
200
CO2
-
pH 7.9, temperature not specified in the publication, the activities depended on culture conditions, ranging between 80/sec and 200/sec
210
CO2
-
pH 7.5, 25°C, variant E62A/E84A, 50 mM MOPS buffer
217
CO2
-
pH 6.28, MES buffer, carbonic anhydrase I mutant V62N
217
CO2
-
pH 6.3, MES buffer
233
CO2
-
pH 8.88, TAPS buffer, carbonic anhydrase I mutant H200T
250
CO2
-
pH 6.28, MES buffer, carbonic anhydrase I mutant H67N
260
CO2
-
pH 8.5, 25°C, mutant D34A/R36A, MOPS buffer
310
CO2
pH 7.5, 37°C, variant R59C, 100 mM ethylguanidine
320
CO2
pH 7.5, 37°C, variant R59C, 100 mM aminoguanidine
340
CO2
-
pH 7.5, 25°C, variant E62A, 50 mM MOPS-Ac buffer
350
CO2
pH 7.5, 37°C, variant R59A, 100 mM aminoguanidine
410
CO2
-
pH 7.5, 25°C, variant E62Q, 50 mM MOPS buffer
433
CO2
-
pH 8.8, TAPS buffer, wild-type carbonic anhydrase I
510
CO2
-
pH 7.5, 25°C, variant E84Y, 50 mM MOPS buffer
520
CO2
pH 7.5, 37°C, variant R59C
520
CO2
-
pH 8.5, 25°C, mutant D34A/R36A
627
CO2
pH 7.5, 37°C, variant R59Q, 100 mM guanidine hydrochloride
720
CO2
-
pH 7.5, 25°C, variant E84C and E62A, 50 mM MOPS buffer
800
CO2
-
pH 7.21, 1-methylimidazole buffer, wild-type carbonic anhydrase I
800
CO2
-
pH 7.5, 25°C, variant E84A, 50 mM MOPS-Ac buffer
860
CO2
-
pH 7.5, 25°C, variant E62T, 50 mM MOPS buffer
870
CO2
-
pH 7.5, 25°C, variant E84A, 50 mM MOPS buffer
883
CO2
-
pH 7.23, 1-methylimidazole buffer, carbonic anhydrase I mutant H67N
910
CO2
-
pH 7.5, 25°C, variant E62C, 50 mM MOPS buffer
990
CO2
pH 7.5, 37°C, variant R59C, 100 mM methylguanidine
1050
CO2
-
pH 7.5, 25°C, variant E62H, 50 mM MOPS buffer
1070
CO2
-
pH 7.5, 25°C, variant E62A, 50 mM IMID buffer
1080
CO2
-
pH 7.5, 25°C, variant E84S, 50 mM MOPS buffer
1100
CO2
-
pH 8.5, 25°C, mutant D34A, MOPS buffer
1180
CO2
-
pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N and carbonic anhydrase I mutant H67N
1300
CO2
-
pH 7.5, 25°C, variant E84Q, 50 mM MOPS buffer
1380
CO2
-
pH 7.21, 1-methylimidazole buffer, carbonic anhydrase I mutant H200T
1400
CO2
-
pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N,H67N,H200T
1470
CO2
-
pH 8.88, TAPS buffer, carbonic anhydrase I mutant V62N,H67N
1500
CO2
-
pH 8.5, 25°C, mutant D34A/R36A, imidazole buffer
1900
CO2
-
pH 7.5, 25°C, variant E84K, 50 mM MOPS buffer
2000
CO2
-
pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62N
2000
CO2
25°C, mutant enzyme C183S/C188S
2170
CO2
pH 7.5, 37°C, variant R59C, 100 mM guanidine
2250
CO2
pH 7.5, 37°C, variant R59A, 150 mM guanidine
2670
CO2
-
pH 6.6, MES buffer
2700
CO2
pH 7.5, 37°C, variant R59A, 50 mM guanidine
2701
CO2
pH 7.5, 37°C, variant R59A, 50 mM guanidine
2740
CO2
pH 7.5, 37°C, variant R59K, 100 mM guanidine hydrochloride
2830
CO2
-
pH 8.75, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H67N
3000
CO2
-
pH 8.8, TAPS buffer
3270
CO2
pH 7.5, 37°C, variant R59A, 100 mM guanidine
3340
CO2
recombinant full-length CcaA274 enzyme, pH 7.5, 25°C, CO2 hydration reaction
3500
CO2
-
pH 8.77, 1,2-dimethylimidazole buffer, wild-type carbonic anhydrase I
3500
CO2
-
pH 8.72, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62B, H67B
3600
CO2
-
pH 8.5, 25°C, mutant D34E
3670
CO2
-
pH 7.23, 1-methylimidazolebuffer, carbonic anhydrase I mutant V62N,H67N,H200T
3830
CO2
-
enzyme from red muscle sarcoplasmic reticulum
4000
CO2
-
pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant T200H
4170
CO2
-
enzyme from red muscle sarcolemmal membranes
4200
CO2
-
pH 8.5, 25°C, mutant D34A
4700
CO2
-
pH 7.5, 25°C, variant E62D/E84D, 50 mM MOPS buffer
4720
CO2
pH 7.5, 37°C, variant R59K, without guanidine hydrochloride
5500
CO2
-
pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H200T
5690
CO2
pH 7.5, 37°C, variant R59A, 100 mM methylguanidine
5800
CO2
25°C, pH 7.5, mutant enzyme W19N
6170
CO2
-
enzyme from white muscle sarcoplasmic reticulum
6500
CO2
25°C, pH 7.5, mutant enzyme W19F
7100
CO2
-
pH 5.7-9.5, 25°C, wild-type
7140
CO2
pH 7.5, 37°C, variant R59A, 100 mM ethylguanidine
7900
CO2
25°C, pH 7.5, mutant enzyme W19A
8170
CO2
-
pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N62V
8500
CO2
-
pH 8.75, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62N,H67N,H200T
9000
CO2
-
enzyme from white muscle sarcolemmal membranes
9100
CO2
-
pH 8.5, 25°C, mutant D34A, imidazole buffer
9300
CO2
-
pH 6.5, 25°C, wild-type, D2O
9500
CO2
-
pH 7.5, 25°C, variant E84H, 50 mM MOPS buffer
11000
CO2
-
pH 8.5, 25°C, wild-type, MOPS buffer
11000
CO2
isozyme bsCAII, pH 8.3, temperature not specified in the publication
13000
CO2
at 20°C and pH 7.5
13000
CO2
-
pH 8.5, 25°C, wild-type, imidazole buffer
13000
CO2
-
isoform carbonic anhydrase III, at pH 7.4 and 25°C
13700
CO2
recombinant full-length CcaA274 enzyme, pH 9.5, 25°C, CO2 hydration reaction
15000
CO2
-
pH not specified in the publication, 25°C
15200
CO2
-
pH 8.7, 1,2-dimethylimidazole buffer, carbonic anhydrase II
16700
CO2
-
pH 8.9, TAPS buffer, carbonic anhydrase II
16700
CO2
-
pH 7.5, 25°C, wild-type, D2O
16800
CO2
-
pH 7.5, 25°C, variant E62D, 50 mM MOPS buffer
18300
CO2
-
carbonic anhydrase IV, pH above 9
18300
CO2
-
pH-independent turnover
18600
CO2
-
pH 6.5, 25°C, wild-type
20000
CO2
pH 7.5, 37°C, variant R59E, without guanidine hydrochloride
21000
CO2
-
pH 7.5, 25°C, variant E84D, 50 mM MOPS buffer
22000
CO2
25°C, mutant enzyme F198L/C183S/C188S
22600
CO2
-
pH 8.5, 25°C, wild-type, D2O
22900
CO2
pH 7.5, 37°C, wild-type, 100 mM guanidine hydrochloride
24000
CO2
-
pH 8.5, 25°C, wild-type
24700
CO2
-
pH 7.5, 25°C, wild-type, 50 mM MOPS-Ac buffer
26500
CO2
-
pH 7.5, 25°C, variant E88A, 50 mM MOPS buffer
28300
CO2
-
pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N67H
29100
CO2
-
pH 7.5, 25°C, variant E89A, 50 mM MOPS buffer
31000
CO2
recombinant truncated CcaA220 enzyme, pH 9.5, 25°C, CO2 hydration reaction
32400
CO2
25°C, pH 7.5, wild-type enzyme
35100
CO2
-
pH 7.5, 25°C, variant E84A, 50 mM IMID buffer
56800
CO2
-
pH 7.5, 25°C, wild-type, 50 mM MOPS buffer
58900
CO2
-
pH 8.5, 25°C, wild-type
62900
CO2
pH 7.5, 37°C, wild-type, without guanidine hydrochloride
64000
CO2
isozyme bsCAI, pH 8.3, temperature not specified in the publication
71900
CO2
-
pH 7.5, 25°C, wild-type, 50 mM IMID buffer
79300
CO2
25°C, pH 7.5, mutant enzyme Y200S
83000
CO2
-
isoform carbonic anhydrase XIII, at pH 7.4 and 25°C
95000
CO2
25°C, pH 7.5, mutant enzyme Y200A
120000
CO2
-
pH 7.5, 20°C
120100
CO2
25°C, pH 7.5, mutant enzyme Y200F
130000
CO2
-
pH 7.5, 20°C
130000
CO2
measured with hydration of CO2 activity assay, pH 7.5-8.3, 0°C
140000
CO2
pH 7.5, 22°C, truncated form PfCA1, CO2 hydration reaction
150000
CO2
-
isoform carbonic anhydrase XIII, at pH 7.4 and 25°C
200000
CO2
-
isoform carbonic anhydrase I, at pH 7.4 and 25°C
240000
CO2
-
pH 8.9, 25°C
280000
CO2
pH 8.3, 22°C, recombinant His-tagged enzyme
310000
CO2
at 20°C and pH 7.5 in 10 mM HEPES buffer
320000
CO2
pH 7.8, 25°C, recombinant enzyme
340000
CO2
-
in the absence of L-Trp and D-Trp, at 25°C and pH 7.5
380000
CO2
-
Escherichia coli recombinant enzyme
380000
CO2
pH 7.5, 22°C, long enzyme form PfCAdom, CO2 hydration reaction
390000
CO2
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
390000
CO2
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
390000
CO2
-
Can2, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
400000
CO2
-
acrolein-modified enzyme
410000
CO2
-
pH 8.3, 20°C
410000
CO2
CO2 hydration, pH 8.3, 22°C, native enzyme
420000
CO2
CO2 hydration, pH 8.3, 22°C, recombinant enzyme
430000
CO2
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
450000
CO2
-
truncated form of carbonic anhydrase VII lacking the amino-terminal 23 residues of recombinant enzyme
470000
CO2
at 20°C and pH 7.5
470000
CO2
-
at pH 7.5 and 20°C
480000
CO2
pH 8.3, 20°C, recombinant His-tagged enzyme
640000
CO2
at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl
640000
CO2
in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
640000
CO2
-
in the presence of 0.01 mM D-Trp, at 25°C and pH 7.5
680000
CO2
-
Can2, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine
685000
CO2
-
purified recombinant CAH-4a, pH 7.5, 4°C
800000
CO2
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
800000
CO2
-
CaNce103, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
813600
CO2
recombinant enzyme, at 4°C in a HEPES/NaOH, pH 7.5
823000
CO2
-
pH 7.5, 20°C
860000
CO2
-
pH 8.3, 20°C
900000
CO2
-
pH 7.5, 20°C
920000
CO2
-
in the presence of 0.01 mM L-Trp, at 25°C and pH 7.5
935000
CO2
-
pH 7.5, 20°C
940000
CO2
-
carbonic anhydrase VII
940000
CO2
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
940000
CO2
-
pH not specified in the publication, temperature not specified in the publication
950000
CO2
-
pH 7.5, 20°C
950000
CO2
-
pH 8.3, 20°C
1000000
CO2
-
pH 7.5, 20°C, mutant Q92V
1100000
CO2
recombinant extracellular domain of CA IX expressed in Sf9 cells, in the absence of Zn2+
1200000
CO2
-
pH 7.5, 20°C
1200000
CO2
-
pH 7.4, 30°C, CO2 hydration activity
1210000
CO2
-
pH 7.5, 20°C
1300000
CO2
-
pH 7.5, 20°C
1400000
CO2
-
pH 7.5, 20°C, wild-type
1400000
CO2
-
isoform carbonic anhydrase II, at pH 7.4 and 25°C
1400000
CO2
-
native isozyme carbonic anhydrase II, in 10 mM HEPES, 0.1 M Na2SO4, pH 7.5
1400000
CO2
-
pH 7.5, 20°C, mutant N67I
1500000
CO2
-
pH 7.5, 20°C, mutant L204S
2010000
CO2
-
CaNce103, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine
3800000
CO2
recombinant CA IX catalytic domain expressed in Escherichia coli
3800000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the absence of Zn2+
4200000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Zn2+
4400000
CO2
-
pH 7.5, 25°C, without activator
4400000
CO2
pH 7.5, 20°C, recombinant His-tagged enzyme
11000000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Mg2+
12000000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Co2+
15000000
CO2
-
pH 7.5, 25°C, 10 microM L-Phe
25000000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Mn2+
25000000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of Zn2+
33000000
CO2
-
pH 7.5, 25°C, 10 microM D-Phe
688
H2CO3
-
pH 9.0, 40°C
13000
H2CO3
-
pH not specified in the publication, 4°C, assay using the delta pH method
29500
H2CO3
-
without NaCl
38300
H2CO3
-
without NaCl
39400
H2CO3
pH 6.8, in absence of NaCl
41200
H2CO3
-
0.25 M NaCl
41600
H2CO3
pH 6.8, 0.1 M NaCl
45000
H2CO3
pH 6.8, 0.5 M NaCl
68000
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and aerobically purified
121500
H2CO3
recombinant enzyme, at 4°C in a MES/KOH pH 6.3 buffer
140000
H2CO3
truncated mutant PfCA1, pH 8.3, 22°C
231000
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Methanosarcina acetivorans and anaerobically purified
243000
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and anaerobically purified
320000
H2CO3
pH 7.5, 20°C
380000
H2CO3
enzyme PfCAdom, pH 8.3, 22°C
890000
H2CO3
carbonate dehydratase activity, recombinant enzyme, pH and temperature not specified in the publication
935000
H2CO3
pH 7.5, 20°C
1400000
H2CO3
pH 7.5, 20°C
1600000
H2CO3
pH 7.5, 20°C
4400000
H2CO3
-
pH 7.5, 20°C
46000
HCO3-
-
pH 7.0, rCsoSCA
380000
histamine
-
at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
1070000
histamine
-
at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine
additional information
additional information
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-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
influence of buffer composition and pH on the turnover-number
-
additional information
additional information
-
influence of pH-value and buffer composition and the native enzyme and on an activated derivative with modified thiol groups
-
additional information
additional information
-
20.3/s with 4-nitrophenyl acetate, pH 9.0, 30°C, esterase activity
-
additional information
additional information
-
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
-
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme
-
additional information
additional information
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme
-
additional information
additional information
-
first order kinetic constant at 25°C is 9160000 L/(mol s)
-