Ligand sulfite

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

Basic Ligand Information

Molecular Structure
Picture of sulfite (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
H2O3S
sulfite
LSNNMFCWUKXFEE-UHFFFAOYSA-L
Synonyms:
(HSO3)-, bisulfite, HSO3-, hydrogen sulfite, hydrogensulfite, SO32-, sulfurous acid, Sulphite
Pathway Source
Pathways
BRENDA
coenzyme M biosynthesis, cysteine metabolism, non-pathway related, sulfate reduction, sulfolipid biosynthesis more
KEGG
Cysteine and methionine metabolism, Microbial metabolism in diverse environments, Sulfur metabolism, Taurine and hypotaurine metabolism
MetaCyc
(R)-cysteate degradation, 3,3'-disulfanediyldipropannoate degradation, 3,3'-thiodipropanoate degradation, 3-sulfopropanediol degradation III, 4-sulfocatechol degradation more


Show all pahtways known for Show all BRENDA pathways known for sulfite

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (30 results)

top print hide
EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
sulfite + reduced coenzyme F420 = hydrogen sulfide + oxidized coenzyme F420
-
show the reaction diagram
sulfite + 6 ferrocytochrome c + 6 H+ = sulfide + 6 ferricytochrome c + 3 H2O
-
show the reaction diagram
O-acetyl-L-serine + sulfite = L-cysteine sulfonate + acetate
-
show the reaction diagram
2-hydroxybiphenyl + sulfite = 2'-hydroxybiphenyl-2-sulfinate + H2O
-
show the reaction diagram
L-Cys + sulfite = ?
-

In Vivo Product in Enzyme-catalyzed Reactions (44 results)

top print hide
EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
-
show the reaction diagram
4-sulfobenzoate + NADH + O2 = 3,4-dihydroxybenzoate + sulfite + NAD+
-
-
show the reaction diagram
thiosulfate + 2 ferrocytochrome c3 = sulfite + hydrogen sulfide + 2 ferricytochrome c3
-
-
show the reaction diagram
hydrogen sulfide + oxidized ferredoxin + H2O = sulfite + reduced ferredoxin + H+
-
-
show the reaction diagram
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O = sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
show the reaction diagram
2-sulfoacetaldehyde + phosphate = acetyl phosphate + sulfite
-
-
show the reaction diagram
thiosulfate + cyanide = sulfite + thiocyanate
-
show the reaction diagram
thiosulfate + glutathione = sulfite + glutathione disulfide + sulfide
-
-
show the reaction diagram
thiosulfate + 2 dithioerythritol = sulfite + dithioerythritol disulfide + sulfide
-
-
show the reaction diagram
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
-
-
show the reaction diagram
3-sulfolactate = pyruvate + bisulfite
-
-
show the reaction diagram
L-cysteate + H2O = pyruvate + bisulfite + NH3
-
-
show the reaction diagram
2-hydroxyethane-1-sulfonate = acetaldehyde + H+ + sulfite
-
-
show the reaction diagram
(2S)-2,3-dihydroxypropane-1-sulfonate = hydroxyacetone + sulfite
-

Substrate in Enzyme-catalyzed Reactions (100 results)

top print hide
EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
glutathione + sulfite + 2 H+ = S-sulfanylglutathione + O2 + H2O
-
show the reaction diagram
sulfite + hydrogen sulfide + menaquinone = thiosulfate + menaquinol
-
show the reaction diagram
sulfite + ferricyanide = sulfate + ferrocyanide
-
show the reaction diagram
O-acetyl-L-serine + sulfite = L-cysteine sulfonate + acetate
-
show the reaction diagram
L-phosphoserine + sulfite = L-cysteate + phosphate
-
show the reaction diagram
thiosulfate + sulfite = sulfite + thiosulfate
show the reaction diagram
2-hydroxybiphenyl + sulfite = 2'-hydroxybiphenyl-2-sulfinate + H2O
-

Product in Enzyme-catalyzed Reactions (158 results)

top print hide
EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
3-sulfocatechol + O2 + H2O = (2E,4Z)-2-hydroxymuconate + bisulfite + H+
-
show the reaction diagram
4-sulfobenzoate + NADH + O2 = 3,4-dihydroxybenzoate + sulfite + NAD+
-
-
show the reaction diagram
thiosulfate + menaquinol = sulfite + hydrogen sulfide + menaquinone
-
-
show the reaction diagram
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O = sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
-
show the reaction diagram
2-sulfoacetaldehyde + phosphate = acetyl phosphate + sulfite
-
-
show the reaction diagram
4-aminobutyrate + 2-oxoglutarate = L-glutamate + acetaldehyde + sulfite
-
show the reaction diagram
L-cysteine sulfinic acid = L-alanine + sulfite
-
-
show the reaction diagram
4-sulfomuconolactone + H2O = maleylacetate + sulfite
-
-
show the reaction diagram
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
-
-
show the reaction diagram
(2S)-2,3-dihydroxypropane-1-sulfonate = hydroxyacetone + sulfite
-

Activator in Enzyme-catalyzed Reactions (19 results)

top print hide
COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (139 results)

top print hide
COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
in decarboxylation of malate: partially competitive with respect to malate, in carboxylation of pyruvate: fully competitive for CO2 or HCO3-
-
competitive
sulfite build up can potentially inhibit PDO activity
-
irreversible inactivation is Cu2+-dependent
-
37.5% inhibtion at 15 mM after 6 h incubation of cells
-
inhibition of activity with NADP+ but not with methyl viologen
-
non-competitive inhibitor with respect to both NADPH and 3-phosphoglycerate
-
in presence of substrate
-
4 mM, 16% residual activity
-
4 mM, 56% residual activity
-
competitive inhibitor
-
competitive, cocrystal structure
-
dead end inhibitor, competitive
-
strong inhibitor, competitive with respect to phosphonate, uncompetitive with respect to NAD+
-
strong inhibitor, competitive with respect to posphonate
-
2 mM sodium sulfite: complete inhibition
-
20 mM, residual activity 53%
-
uncompetitive
-
uncompetitive vs. hydroxylamine
-
1 mM, 22% inhibition
-
24% inhibition at 10 mM
1 mM, 30% inhibition
-
100% inhibition at 0.5 mM
2 mM, 1.6fold stimulation. Inhibitory at higher concentrations, almost complete inhibition at 10 mM
50% inhibition at 0.005 mM , time-dependent inhibition, irreversible
50% inhibition at 1.7 mM
62% inhibition at 3 mM
75% inhibition at 1 mM, 48% inhibition at 0.1 mM 33% inhibition at 0.01 mM
inhibits at concentrations above 0.05 mM, the sulfite inhibition of thiosulfate oxidation by whole cells is very similar to the inhibition pattern of the enzyme
strongly inhibits, the inhibition is time-dependent and irreversible, 50% inhibition at 0.005 mM in 5 min
preincubation of SoxF with 1 mM sodium sulfite for 20 min inactivates SoxF (9.0% residual sulfide dehydrogenase activity)
-
3 mM, 45% inhibition
-
0.005 mM, 48% inhibition, 0.05 mM, complete inhibition
-
almost complete inhibition in the presence of 10 mM sulfite
-
activates 1.6fold at 2 mM, higher concentration of sulfite ions results in inhibition of the enzyme, and almost complete inhibition at 10 mM sulfite
-
0.1 mM, complete inhibition
-
above 1 mM, product inhibition
-
competitive to sulfide
-
1 mM, 10-25% inhibition
-
competitive inhibition against thiosulfate in untreated mice, activating effect activity at high thiosulfate concentrations in p-dimethylaminoazobenzene-treated mice
H2S production by the enzyme is suppressed by sulfite
competitive inhibition when glutathione is the varied substrate
-
competitive with respect to dithiothreitol, non-competitive with respect to thiosulfate
-
product inhibition, competitive versus both substrates
-
enzymatic activity: 1.6%
-
inhibites phytase activity
-
potent inhibitor
-
0.2 mM 97% inhibition
-
competitive inhibitor
increasing concentrations beyond 0.1 mM
-
reversible
-
inhibitory effect increases rapidly with time to a constant level, not competitve with substrate
-
competitive inhibitor. The structure of the urease-sulfite complex, determined at 1.65 A resolution, shows the inhibitor bound to the dinuclear Ni(II) center of urease in a tridentate mode involving bonds between the two Ni(II) ions in the active site and all three oxygen atoms of the inhibitor
noncompetitive, inhibition by a time-dependent mechanism, addition of succinic semialdehyde protects against sulfite inhibition
-
inhibitory at 20 mM
-
complete inhibition at 1.0 mM
-
shows low micromolar inhibition against CA XV
weak inhibitor of the Zn(II)-substituted enzyme
NaHSO3
-
10 mM, 95% loss of activity after 90 min, 0.1 mM 1-amino-2-imidazol-4'-ylethylphosphoric acid protects
-
sodiumbisulfite
-
substrate inhibition above 3 mM
-
noncompetitive
-

Metals and Ions (7 results)

top print hide
COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
binds at the active site as arsenite analogue
-
activates 1.6fold at 2 mM, higher concentration of sulfite ions results in inhibition of the enzyme, and almost complete inhibition at 10 mM sulfite
-
stimulates
-
activates
-
reduction is essential for catalytic activity
-
K2SO3, absolute requirement in the reactivation of the inactive enzyme complex with hydroxocobalamin
-

3D Structure of Enzyme-Ligand-Complex (PDB) (248 results)

top print hide
EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (225 results)

top print hide
COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
modified enzyme that contains an additional covalent bond between residues Tyr303 and Gln360, pH 7.0, 20°C
0.023
-
unmodified enzyme, pH 7.0, 20°C
0.039
-
cosubstrate NADPH
30
40
cosubstrate reduced methyl viologen
65
-
25°C, 20 mM Tris acetate buffer, pH 10.0, mutant Y236F
88.8
-
25°C, 20 mM Tris acetate buffer, pH 10.0, wild-type enzyme
2
3.7
25°C, 20 mM Tris acetate buffer, pH 5.8, mutant R55M
70.5
-
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant H57A
238.8
-
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant Y236F
36.8
-
25°C, 20 mM Tris acetate buffer, pH 6.0, wild-type enzyme
63.5
-
25°C, 20 mM Tris acetate buffer, pH 6.2, mutant R55M
64
-
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant H57A
226.5
-
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant Y236F
41.6
-
25°C, 20 mM Tris acetate buffer, pH 6.5, wild-type enzyme
86.2
-
25°C, 20 mM Tris acetate buffer, pH 6.6, mutant R55M
64
-
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant H57A
214.5
-
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant R55M
66.3
-
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant Y236F
51.8
-
25°C, 20 mM Tris acetate buffer, pH 7.0, wild-type enzyme
158.8
-
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant H57A
220.5
-
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant R55M
68.3
-
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant Y236F
48.3
-
25°C, 20 mM Tris acetate buffer, pH 7.5, wild-type enzyme
293.4
-
25°C, 20 mM Tris acetate buffer, pH 7.9, mutant R55M
73.4
-
25°C, 20 mM Tris acetate buffer, pH 8.0, mutant H57A
214.6
-
25°C, 20 mM Tris acetate buffer, pH 8.0, mutant Y236F
53.4
-
25°C, 20 mM Tris acetate buffer, pH 8.0, wild-type enzyme
345.3
-
25°C, 20 mM Tris acetate buffer, pH 8.5, mutant H57A
222.4
-
25°C, 20 mM Tris acetate buffer, pH 8.5, mutant Y236F
58.3
-
25°C, 20 mM Tris acetate buffer, pH 8.5, wild-type enzyme
410
-
25°C, 20 mM Tris acetate buffer, pH 9.0, mutant H57A
192.5
-
25°C, 20 mM Tris acetate buffer, pH 9.0, mutant Y236F
64
-
25°C, 20 mM Tris acetate buffer, pH 9.0, wild-type enzyme
519
-
25°C, 20 mM Tris acetate buffer, pH 9.5, mutant H57A
148.4
-
25°C, 20 mM Tris acetate buffer, pH 9.5, mutant Y236F
52.7
-
25°C, 20 mM Tris acetate buffer, pH 9.5, wild-type enzyme
431
-
mutant enzyme P105A, in 20 mM Tris acetate, pH 8.0, at 25°C
39
-
mutant enzyme P105A/P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
46
-
mutant enzyme P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
50
-
mutant enzyme Y236F, in 20 mM bis-Tris-acetate buffer pH 6.0
mutant enzyme Y236F, in 20 mM Tris-acetate buffer pH 8.0
recombinant enzyme
10880
-
tether deletion mutant enzyme DELTAKVA, in 20 mM Tris acetate, pH 8.0, at 25°C
40
-
tether deletion mutant enzyme DELTAKVAT, in 20 mM Tris acetate, pH 8.0, at 25°C
35
-
tether deletion mutant enzyme DELTAKVATV, in 20 mM Tris acetate, pH 8.0, at 25°C
10.6
-
wild type enzyme, in 20 mM bis-Tris-acetate buffer pH 6.0
33.51
-
wild type enzyme, in 20 mM Tris acetate, pH 8.0, at 25°C
26.9
-
wild type enzyme, in 20 mM Tris-acetate buffer pH 8.0
333.7
-
25°C, pH 10.0, 100 mM buffer, mutant enzyme Y343F
8.21
-
25°C, pH 10.0, 20 mM buffer, mutant enzyme Y343F
8.51
-
25°C, pH 6.0, 20 mM buffer, mutant enzyme Y343F
3.11
-
25°C, pH 6.0, 20 mM buffer, wild-type enzyme
13.2
-
25°C, pH 6.5, 20 mM buffer, mutant enzyme Y343F
4.14
-
25°C, pH 6.5, 20 mM buffer, wild-type enzyme
17.7
-
25°C, pH 7.0, 100 mM buffer, mutant enzyme Y343F
2.06
-
25°C, pH 7.0, 100 mM buffer, wild-type enzyme
12.1
-
25°C, pH 7.0, 20 mM buffer, mutant enzyme Y343F
4.59
-
25°C, pH 7.0, 20 mM buffer, wild-type enzyme
24.2
-
25°C, pH 7.5, 100 mM buffer, mutant enzyme Y343F
3.26
-
25°C, pH 7.5, 100 mM buffer, wild-type enzyme
17.2
-
25°C, pH 7.5, 20 mM buffer, mutant enzyme Y343F
6.35
-
25°C, pH 7.5, 20 mM buffer, wild-type enzyme
24.7
-
25°C, pH 8.0, 100 mM buffer, mutant enzyme Y343F
7.17
-
25°C, pH 8.0, 100 mM buffer, wild-type enzyme
25
-
25°C, pH 8.0, 20 mM buffer, mutant enzyme Y343F
8.59
-
25°C, pH 8.0, 20 mM buffer, wild-type enzyme
25.9
-
25°C, pH 8.25, 100 mM buffer, mutant enzyme Y343F
8.72
-
25°C, pH 8.25, 100 mM buffer, wild-type enzyme
27
-
25°C, pH 8.25, 20 mM buffer, mutant enzyme Y343F
9.08
-
25°C, pH 8.25, 20 mM buffer, wild-type enzyme
24.8
-
25°C, pH 8.5, 100 mM buffer, mutant enzyme Y343F
9.2
-
25°C, pH 8.5, 100 mM buffer, wild-type enzyme
26.9
-
25°C, pH 8.5, 20 mM buffer, mutant enzyme Y343F
9.24
-
25°C, pH 8.5, 20 mM buffer, wild-type enzyme
26.9
-
25°C, pH 8.75, 20 mM buffer, wild-type enzyme
23.6
-
25°C, pH 9.0, 100 mM buffer, mutant enzyme Y343F
9.99
-
25°C, pH 9.0, 100 mM buffer, wild-type enzyme
28.1
-
25°C, pH 9.0, 20 mM buffer, mutant enzyme Y343F
9.47
-
25°C, pH 9.0, 20 mM buffer, wild-type enzyme
25.7
-
25°C, pH 9.5, 100 mM buffer, mutant enzyme Y343F
10.5
-
25°C, pH 9.5, 100 mM buffer, wild-type enzyme
24.6
-
25°C, pH 9.5, 20 mM buffer, mutant enzyme Y343F
9.63
-
25°C, pH 9.5, 20 mM buffer, wild-type enzyme
26.3
-
25°C, pH 9.75, 20 mM buffer, mutant enzyme Y343F
9.92
-
mutant D342K, pH 7.6, 25°C
23
-
mutant enzyme A208D in 20 mM Tris at pH 6.0
0.15
-
mutant enzyme A208D in 20 mM Tris at pH 8.5
0.75
-
mutant enzyme G473A in 20 mM Tris at pH 6.0
4.15
-
mutant enzyme G473A in 20 mM Tris at pH 8.5
28.4
-
mutant enzyme G473A, pH 10.0
15.1
-
mutant enzyme G473A, pH 6.0
4.15
-
mutant enzyme G473A, pH 7.0
15.9
-
mutant enzyme G473A, pH 7.4
21.6
-
mutant enzyme G473A, pH 8.0
26.2
-
mutant enzyme G473A, pH 8.5
28.4
-
mutant enzyme G473A, pH 9.1
31.9
-
mutant enzyme G473D in 20 mM Tris at pH 6.0
0.14
-
mutant enzyme G473D in 20 mM Tris at pH 8.5
0.54
-
mutant enzyme G473D, pH 6.0
0.14
-
mutant enzyme G473D, pH 6.5
0.28
-
mutant enzyme G473D, pH 7.0
0.5
-
mutant enzyme G473D, pH 7.5
0.57
-
mutant enzyme G473D, pH 8.0
0.58
-
mutant enzyme G473D, pH 8.5
0.54
-
mutant enzyme G473D, pH 9.1
0.42
-
mutant enzyme G473W in 20 mM Tris at pH 6.0
0.6
-
mutant enzyme G473W in 20 mM Tris at pH 8.5
2.48
-
mutant enzyme G473W, pH 6.0
0.6
-
mutant enzyme G473W, pH 7.0
1.8
-
mutant enzyme G473W, pH 8.5
2.48
-
mutant enzyme G473W, pH 9.0
1.35
-
mutant F57A, pH 8.0, 25°C
16
-
mutant F57Y, pH 8.0, 25°C
19
-
mutant F79A, pH 8.0, 25°C
13
-
mutant H90F, pH 8.0, 25°C
19
-
mutant H90Y, pH 8.0, 25°C
42
-
mutant R472D, pH 6.5, 25°C
5.7
-
mutant R472D, pH 7.6, 25°C
14.1
-
mutant R472D/D342K, pH 7.6, 25°C
47
-
mutant R472K, pH 7.6, 25°C
18.5
-
mutant R472M, 25°C, pH 10.0
0.46
-
mutant R472M, 25°C, pH 6.0
5
-
mutant R472M, 25°C, pH 7.0
3.6
-
mutant R472M, 25°C, pH 8.0
3.5
-
mutant R472M, 25°C, pH 8.5
3.8
-
mutant R472M, 25°C, pH 9.0
3.45
-
mutant R472M, 25°C, pH 9.5
1.8
-
mutant R472M, pH 7.6, 25°C
27
-
mutant R472Q, 25°C, pH 10.0
0.52
-
mutant R472Q, 25°C, pH 6.0
8.2
-
mutant R472Q, 25°C, pH 7.0
5.8
-
mutant R472Q, 25°C, pH 8.0
9.3
-
mutant R472Q, 25°C, pH 8.5
4.6
-
mutant R472Q, 25°C, pH 9.0
4.24
-
mutant R472Q, 25°C, pH 9.5
1.7
-
mutant R472Q, pH 7.6, 25°C
26.6
-
mutant V474M, 25°C, pH 10.0
12.4
-
mutant V474M, 25°C, pH 6.0
5.96
-
mutant V474M, 25°C, pH 7.0
11.4
-
mutant V474M, 25°C, pH 8.0
17.8
-
mutant V474M, 25°C, pH 8.5
15.8
-
mutant V474M, 25°C, pH 9.0
19.6
-
mutant V474M, 25°C, pH 9.5
17.1
-
mutant Y322N/R450M, 25°C, pH 7.0
4.83
-
mutant Y322N/R450M, 25°C, pH 8.5
2.52
-
mutant Y343F/R472Q, 25°C, pH 10.0
2.96
-
mutant Y343F/R472Q, 25°C, pH 6.0
1.44
-
mutant Y343F/R472Q, 25°C, pH 7.0
1.73
-
mutant Y343F/R472Q, 25°C, pH 8.0
2.05
-
mutant Y343F/R472Q, 25°C, pH 8.5
2.25
-
mutant Y343F/R472Q, 25°C, pH 9.0
2.3
-
mutant Y343F/R472Q, 25°C, pH 9.5
4.9
-
mutant Y343N, 25°C, pH 10.0
4.38
-
mutant Y343N, 25°C, pH 6.0
3.17
-
mutant Y343N, 25°C, pH 7.0
12.8
-
mutant Y343N, 25°C, pH 8.0
13.75
-
mutant Y343N, 25°C, pH 8.5
16.9
-
mutant Y343N, 25°C, pH 9.0
15.5
-
mutant Y343N, 25°C, pH 9.5
8.1
-
mutant Y343N/R472M/V474M, 25°C, pH 10.0
2.8
-
mutant Y343N/R472M/V474M, 25°C, pH 6.0
1.9
-
mutant Y343N/R472M/V474M, 25°C, pH 7.0
3.4
-
mutant Y343N/R472M/V474M, 25°C, pH 8.0
3.58
-
mutant Y343N/R472M/V474M, 25°C, pH 8.5
3.9
-
mutant Y343N/R472M/V474M, 25°C, pH 9.0
5.6
-
mutant Y343N/R472M/V474M, 25°C, pH 9.5
5.23
-
mutant Y343N/R472Q, 25°C, pH 6.0
1.35
-
mutant Y343N/R472Q, 25°C, pH 7.0
1.13
-
mutant Y343N/R472Q, 25°C, pH 8.0
1.33
-
mutant Y343N/R472Q, 25°C, pH 8.5
1.42
-
mutant Y343N/R472Q, 25°C, pH 9.0
1.13
-
mutant Y343N/R472Q, 25°C, pH 9.5
0.97
-
mutant Y83A, pH 8.0, 25°C
7
-
mutant Y83F, pH 8.0, 25°C
3
6
wild type enzyme in 20 mM Tris at pH 6.0
13.2
-
wild type enzyme in 20 mM Tris at pH 8.5
26.9
-
wild type enzyme, pH 6.0
13.2
-
wild type enzyme, pH 6.5
17.7
-
wild type enzyme, pH 7.0
24.2
-
wild type enzyme, pH 7.5
24.7
-
wild type enzyme, pH 8.0
25.9
-
wild type enzyme, pH 8.5
26.9
-
wild type enzyme, pH 9.0
25.7
-
wild type enzyme, pH 9.5
26.3
-
wild-type, 25°C, pH 10.0
13
-
wild-type, 25°C, pH 6.0
13.2
-
wild-type, 25°C, pH 7.0
wild-type, 25°C, pH 8.0
25.9
-
wild-type, 25°C, pH 8.5
wild-type, 25°C, pH 9.0
25.7
-
wild-type, 25°C, pH 9.5
26.3
-
wild-type, pH 8.0, 25°C
with ferricanide, pH 6.0, 25°C, recombinant mutant C242S/C253S/C260S/C451S
9.4
-
with ferricanide, pH 6.0, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
26.1
-
with ferricanide, pH 6.0, 25°C, recombinant wild-type enzyme
13.9
-
with ferricanide, pH 7.1, 25°C, recombinant mutant C242S/C253S/C260S/C451S
19.8
-
with ferricanide, pH 7.1, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
with ferricanide, pH 7.1, 25°C, recombinant wild-type enzyme
with ferricanide, pH 8.4, 25°C, recombinant mutant C242S/C253S/C260S/C451S
25.8
-
with ferricanide, pH 8.4, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
41.2
-
with ferricanide, pH 8.4, 25°C, recombinant wild-type enzyme
32.4
-
with ferricanide, pH 8.9, 25°C, recombinant mutant C242S/C253S/C260S/C451S
36.2
-
with ferricanide, pH 8.9, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
31.8
-
with ferricanide, pH 8.9, 25°C, recombinant wild-type enzyme
27.3
-
cosubstrates sulfide, ubiquinone-1, pH 7.5, 25°C
368
-
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
368
-
enzyme in nanodiscs, at pH 6.8 and 25°C
650
-
solubilized enzyme, at pH 6.8 and 25°C
382
-
-
4.7
-
leaf enzyme
9.1
-
mutant G212S/L213T/Y214L/S217C/C220I/S221N, pH not specified in the publication, temperature not specified in the publication
0.133
-
root enzyme
2.4
-
truncated protein, residues 19-731, pH not specified in the publication, temperature not specified in the publication
1.93
-
truncated protein, residues 76-679, pH not specified in the publication, temperature not specified in the publication
0.078
-
pH 7.6, 22°C
0.31
-

KM Value (289 results)

top print hide
COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
in 0.1 M K+-phosphate buffer, at pH 7.0 and 30°C
60
-
within a sulfite concentration range of 0.0014-0.3 mM and with a fixed reduced F420 concentration of 0.04 mM
0.0122
-
25°C, 20 mM Tris acetate buffer, pH 10.0, mutant Y236F
15.49
-
25°C, 20 mM Tris acetate buffer, pH 10.0, wild-type enzyme
3.39
-
25°C, 20 mM Tris acetate buffer, pH 5.8, mutant R55M
0.812
-
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant H57A
0.667
-
25°C, 20 mM Tris acetate buffer, pH 6.0, mutant Y236F
0.000004
-
25°C, 20 mM Tris acetate buffer, pH 6.0, wild-type enzyme
0.0006
-
25°C, 20 mM Tris acetate buffer, pH 6.2, mutant R55M
1.087
-
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant H57A
0.29
-
25°C, 20 mM Tris acetate buffer, pH 6.5, mutant Y236F
0.000007
-
25°C, 20 mM Tris acetate buffer, pH 6.5, wild-type enzyme
0.0011
-
25°C, 20 mM Tris acetate buffer, pH 6.6, mutant R55M
1.63
-
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant H57A
0.189
-
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant R55M
1.95
-
25°C, 20 mM Tris acetate buffer, pH 7.0, mutant Y236F
0.026
-
25°C, 20 mM Tris acetate buffer, pH 7.0, wild-type enzyme
0.0037
-
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant H57A
0.22
-
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant R55M
3.62
-
25°C, 20 mM Tris acetate buffer, pH 7.5, mutant Y236F
0.042
-
25°C, 20 mM Tris acetate buffer, pH 7.5, wild-type enzyme
0.0071
-
25°C, 20 mM Tris acetate buffer, pH 7.9, mutant R55M
8.17
-
25°C, 20 mM Tris acetate buffer, pH 8.0, mutant H57A
0.27
-
25°C, 20 mM Tris acetate buffer, pH 8.0, mutant Y236F
0.114
-
25°C, 20 mM Tris acetate buffer, pH 8.0, wild-type enzyme
0.022
-
25°C, 20 mM Tris acetate buffer, pH 8.5, mutant H57A
0.452
-
25°C, 20 mM Tris acetate buffer, pH 8.5, mutant Y236Fyme
0.332
-
25°C, 20 mM Tris acetate buffer, pH 8.5, wild-type enzyme
0.086
-
25°C, 20 mM Tris acetate buffer, pH 9.0, mutant H57A
1.46
-
25°C, 20 mM Tris acetate buffer, pH 9.0, mutant Y236F
1.155
-
25°C, 20 mM Tris acetate buffer, pH 9.0, wild-type enzyme
0.324
-
25°C, 20 mM Tris acetate buffer, pH 9.5, mutant H57A
12.2
-
25°C, 20 mM Tris acetate buffer, pH 9.5, mutant Y236F
4.456
-
25°C, 20 mM Tris acetate buffer, pH 9.5, wild-type enzyme
1.66
-
at pH 7.7 and 294 mV
0.012
-
at pH 7.7 and 360 mV
0.0125
-
at pH 8.0 and 264 mV
0.063
-
at pH 8.0 and 345 mV
0.054
-
at pH 8.5 and 283 mV
0.283
-
at pH 8.5 and 345 mV
0.269
-
mutant enzyme G473A, pH 7.0, using ferricyanide as the electron acceptor
0.00605
-
mutant enzyme G473A, pH 8.5, using ferricyanide as the electron acceptor
0.191
-
mutant enzyme G473D, pH 7.0, using ferricyanide as the electron acceptor
26.5
-
mutant enzyme G473D, pH 8.5, using ferricyanide as the electron acceptor
41.4
-
mutant enzyme G473W, pH 7.0, using ferricyanide as the electron acceptor
21.2
-
mutant enzyme G473W, pH 8.5, using ferricyanide as the electron acceptor
24
-
mutant enzyme P105A, in 20 mM Tris acetate, pH 8.0, at 25°C
0.006
-
mutant enzyme P105A/P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
0.032
-
mutant enzyme P111A, in 20 mM Tris acetate, pH 8.0, at 25°C
0.033
-
pH 6.5, reaction with cytochrome c
0.002
-
pH 8.0, reaction with cytochrome c
0.04
-
reaction with cytochrome c
reaction with ferricyanide
reaction with yeast ferricytochrome c
0.01
-
recombinant enzyme
0.032
-
tether deletion mutant enzyme DELTAKVA, in 20 mM Tris acetate, pH 8.0, at 25°C
0.042
-
tether deletion mutant enzyme DELTAKVAT, in 20 mM Tris acetate, pH 8.0, at 25°C
0.026
-
tether deletion mutant enzyme DELTAKVATV, in 20 mM Tris acetate, pH 8.0, at 25°C
0.0026
-
wild type enzyme, in 20 mM Tris acetate, pH 8.0, at 25°C
0.0111
-
wild type enzyme, pH 7.0, using ferricyanide as the electron acceptor
0.00456
-
wild type enzyme, pH 8.6, using ferricyanide as the electron acceptor
0.0149
-
25°C, pH 10.0, 100 mM buffer, mutant enzyme Y343F
1.54
-
25°C, pH 10.0, 20 mM buffer, mutant enzyme Y343F
0.00851
-
25°C, pH 6.0, 20 mM buffer, mutant enzyme Y343F
0.00311
-
25°C, pH 6.0, 20 mM buffer, wild-type enzyme
0.00129
-
25°C, pH 6.5, 20 mM buffer, mutant enzyme Y343F
0.00414
-
25°C, pH 6.5, 20 mM buffer, wild-type enzyme
0.00162
-
25°C, pH 7.0, 100 mM buffer, mutant enzyme Y343F
0.00352
-
25°C, pH 7.0, 100 mM buffer, wild-type enzyme
0.00362
-
25°C, pH 7.0, 20 mM buffer, mutant enzyme Y343F
0.00459
-
25°C, pH 7.0, 20 mM buffer, wild-type enzyme
0.00272
-
25°C, pH 7.5, 100 mM buffer, mutant enzyme Y343F
0.00423
-
25°C, pH 7.5, 100 mM buffer, wild-type enzyme
0.00367
-
25°C, pH 7.5, 20 mM buffer, mutant enzyme Y343F
0.00635
-
25°C, pH 7.5, 20 mM buffer, wild-type enzyme
0.00339
-
25°C, pH 8.0, 100 mM buffer, mutant enzyme Y343F
0.0158
-
25°C, pH 8.0, 100 mM buffer, wild-type enzyme
0.00612
-
25°C, pH 8.0, 20 mM buffer, mutant enzyme Y343F
0.00859
-
25°C, pH 8.0, 20 mM buffer, wild-type enzyme
0.00435
-
25°C, pH 8.25, 100 mM buffer, mutant enzyme Y343F
0.0319
-
25°C, pH 8.25, 100 mM buffer, wild-type enzyme
0.00728
-
25°C, pH 8.25, 20 mM buffer, mutant enzyme Y343F
0.00908
-
25°C, pH 8.25, 20 mM buffer, wild-type enzyme
0.00503
-
25°C, pH 8.5, 100 mM buffer, mutant enzyme Y343F
0.0557
-
25°C, pH 8.5, 100 mM buffer, wild-type enzyme
0.011
-
25°C, pH 8.5, 20 mM buffer, mutant enzyme Y343F
0.00924
-
25°C, pH 8.5, 20 mM buffer, wild-type enzyme
0.00825
-
25°C, pH 8.75, 20 mM buffer, wild-type enzyme
0.00959
-
25°C, pH 9.0, 100 mM buffer, mutant enzyme Y343F
0.147
-
25°C, pH 9.0, 100 mM buffer, wild-type enzyme
0.026
-
25°C, pH 9.0, 20 mM buffer, mutant enzyme Y343F
0.00947
-
25°C, pH 9.0, 20 mM buffer, wild-type enzyme
0.0221
-
25°C, pH 9.5, 100 mM buffer, mutant enzyme Y343F
0.59
1
25°C, pH 9.5, 100 mM buffer, wild-type enzyme
0.0536
-
25°C, pH 9.5, 20 mM buffer, mutant enzyme Y343F
0.00963
-
25°C, pH 9.5, 20 mM buffer, wild-type enzyme
0.0671
-
25°C, pH 9.75, 20 mM buffer, mutant enzyme Y343F
0.00992
-
mutant D342K, pH 7.6, 25°C
0.012
-
mutant enzyme A208D in 20 mM Tris at pH 6.0
0.0692
-
mutant enzyme A208D in 20 mM Tris at pH 8.5
1.39
-
mutant enzyme G473A in 20 mM Tris at pH 6.0
0.00453
-
mutant enzyme G473A in 20 mM Tris at pH 8.5
0.107
-
mutant enzyme G473A, pH 10.0
3.684
-
mutant enzyme G473A, pH 6.0
0.00453
-
mutant enzyme G473A, pH 7.0
0.00536
-
mutant enzyme G473A, pH 7.4
0.0172
-
mutant enzyme G473A, pH 8.0
0.0487
-
mutant enzyme G473A, pH 8.5
0.107
-
mutant enzyme G473A, pH 9.1
0.774
-
mutant enzyme G473D in 20 mM Tris at pH 6.0
1.66
-
mutant enzyme G473D in 20 mM Tris at pH 8.5
2.04
-
mutant enzyme G473D, pH 6.0
1.66
-
mutant enzyme G473D, pH 6.5
0.99
-
mutant enzyme G473D, pH 7.0
0.623
-
mutant enzyme G473D, pH 7.5
1.063
-
mutant enzyme G473D, pH 8.0
1.223
-
mutant enzyme G473D, pH 8.5
2.04
-
mutant enzyme G473D, pH 9.1
25.88
-
mutant enzyme G473W in 20 mM Tris at pH 6.0
1.91
-
mutant enzyme G473W in 20 mM Tris at pH 8.5
2.03
-
mutant enzyme G473W, pH 6.0
1.91
-
mutant enzyme G473W, pH 7.0
0.33
-
mutant enzyme G473W, pH 8.5
2.034
-
mutant enzyme G473W, pH 9.0
10.41
-
mutant F57A, pH 8.0, 25°C
0.013
-
mutant F57Y, pH 8.0, 25°C
0.008
-
mutant F79A, pH 8.0, 25°C
0.0038
-
mutant H90F, pH 8.0, 25°C
0.0028
-
mutant H90Y, pH 8.0, 25°C
0.0039
-
mutant R472D, pH 6.5, 25°C
0.051
-
mutant R472D, pH 7.6, 25°C
0.023
-
mutant R472D/D342K, pH 7.6, 25°C
0.023
-
mutant R472K, pH 7.6, 25°C
0.0032
-
mutant R472M, 25°C, pH 10.0
0.0969
-
mutant R472M, 25°C, pH 6.0
0.0019
-
mutant R472M, 25°C, pH 7.0
0.0025
-
mutant R472M, 25°C, pH 8.0
0.0047
-
mutant R472M, 25°C, pH 8.5
0.094
-
mutant R472M, 25°C, pH 9.0
0.021
-
mutant R472M, 25°C, pH 9.5
0.0537
-
mutant R472M, pH 7.6, 25°C
0.042
-
mutant R472Q, 25°C, pH 10.0
0.181
-
mutant R472Q, 25°C, pH 6.0
0.0023
-
mutant R472Q, 25°C, pH 7.0
0.0035
-
mutant R472Q, 25°C, pH 8.0
0.013
-
mutant R472Q, 25°C, pH 8.5
0.016
-
mutant R472Q, 25°C, pH 9.0
0.045
-
mutant R472Q, 25°C, pH 9.5
0.0967
-
mutant R472Q, pH 7.6, 25°C
0.022
-
mutant V474M, 25°C, pH 10.0
0.04
-
mutant V474M, 25°C, pH 6.0
0.00046
-
mutant V474M, 25°C, pH 7.0
0.00134
-
mutant V474M, 25°C, pH 8.0
0.0032
-
mutant V474M, 25°C, pH 8.5
0.0354
-
mutant V474M, 25°C, pH 9.0
0.0144
-
mutant V474M, 25°C, pH 9.5
0.0319
-
mutant Y322N/R450M, 25°C, pH 7.0
8.6
-
mutant Y322N/R450M, 25°C, pH 8.5
11.73
-
mutant Y343F/R472Q, 25°C, pH 10.0
59.6
-
mutant Y343F/R472Q, 25°C, pH 6.0
0.0614
-
mutant Y343F/R472Q, 25°C, pH 7.0
0.0877
-
mutant Y343F/R472Q, 25°C, pH 8.0
0.2827
-
mutant Y343F/R472Q, 25°C, pH 8.5
0.712
-
mutant Y343F/R472Q, 25°C, pH 9.0
3.34
-
mutant Y343F/R472Q, 25°C, pH 9.5
39.9
-
mutant Y343N, 25°C, pH 10.0
12
-
mutant Y343N, 25°C, pH 6.0
0.0953
-
mutant Y343N, 25°C, pH 7.0
0.0947
-
mutant Y343N, 25°C, pH 8.0
0.297
-
mutant Y343N, 25°C, pH 8.5
0.85
-
mutant Y343N, 25°C, pH 9.0
2.46
-
mutant Y343N, 25°C, pH 9.5
9.37
-
mutant Y343N/R472M, 25°C, pH 6.0
16.8
-
mutant Y343N/R472M, 25°C, pH 7.0
4.64
-
mutant Y343N/R472M, 25°C, pH 8.0
19.28
-
mutant Y343N/R472M, 25°C, pH 8.5
42.99
-
mutant Y343N/R472M, 25°C, pH 9.0
85.64
-
mutant Y343N/R472m, 25°C, pH 9.5
208
-
mutant Y343N/R472M/V474M, 25°C, pH 10.0
418
-
mutant Y343N/R472M/V474M, 25°C, pH 6.0
1.1
-
mutant Y343N/R472M/V474M, 25°C, pH 7.0
1.42
-
mutant Y343N/R472M/V474M, 25°C, pH 8.0
2.14
-
mutant Y343N/R472M/V474M, 25°C, pH 8.5
14
-
mutant Y343N/R472M/V474M, 25°C, pH 9.0
55.5
-
mutant Y343N/R472M/V474M, 25°C, pH 9.5
111
-
mutant Y83A, pH 8.0, 25°C
0.0017
-
mutant Y83F, pH 8.0, 25°C
0.012
-
pH not specified in the publication, temperature not specified in the publication
0.0214
-
using ferricyanide as electron acceptor
wild type enzyme in 20 mM Tris at pH 6.0
0.00129
-
wild type enzyme in 20 mM Tris at pH 8.5
0.00825
-
wild type enzyme, pH 6.0
0.00129
-
wild type enzyme, pH 6.5
0.00162
-
wild type enzyme, pH 7.0
0.00272
-
wild type enzyme, pH 7.5
0.00339
-
wild type enzyme, pH 8.0
0.00435
-
wild type enzyme, pH 8.5
0.00825
-
wild type enzyme, pH 9.0
0.0221
-
wild type enzyme, pH 9.5
0.0671
-
wild-type, 25°C, pH 10.0
0.0529
-
wild-type, 25°C, pH 6.0
0.0013
-
wild-type, 25°C, pH 7.0
wild-type, 25°C, pH 8.0
0.0043
-
wild-type, 25°C, pH 8.5
wild-type, 25°C, pH 9.0
0.022
-
wild-type, 25°C, pH 9.5
0.067
-
wild-type, pH 8.0, 25°C
0.011
-
with ferricanide, pH 6.0, 25°C, recombinant mutant C242S/C253S/C260S/C451S
0.0096
-
with ferricanide, pH 6.0, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
0.019
-
with ferricanide, pH 6.0, 25°C, recombinant wild-type enzyme
0.0121
-
with ferricanide, pH 7.1, 25°C, recombinant mutant C242S/C253S/C260S/C451S
with ferricanide, pH 7.1, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
with ferricanide, pH 7.1, 25°C, recombinant wild-type enzyme
with ferricanide, pH 8.4, 25°C, recombinant mutant C242S/C253S/C260S/C451S
0.0107
-
with ferricanide, pH 8.4, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
0.0146
-
with ferricanide, pH 8.4, 25°C, recombinant wild-type enzyme
0.0166
-
with ferricanide, pH 8.9, 25°C, recombinant mutant C242S/C253S/C260S/C451S
0.0288
-
with ferricanide, pH 8.9, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
0.0174
-
with ferricanide, pH 8.9, 25°C, recombinant wild-type enzyme
0.0196
-
cosubstrates sulfide, ubiquinone-1, pH 7.5, 25°C
0.174
-
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
0.174
-
at pH 7.4 and 37°C
0.22
-
enzyme in nanodiscs, at pH 6.8 and 25°C
0.26
-
solubilized enzyme, at pH 6.8 and 25°C
0.19
-
63K enzyme, ferredoxin als electeron donor
0.021
-
63K enzyme, reduced methyl viologen as electron donor
0.011
-
69K enzyme, ferredoxin as electron donor
0.025
-
69K enzyme, reduced methyl viologen as electron donor
0.012
-
leaf enzyme
0.22
-
mutant G212S/L213T/Y214L/S217C/C220I/S221N, pH not specified in the publication, temperature not specified in the publication
0.0064
-
root enzyme
0.2
-
truncated protein, residues 19-731, pH not specified in the publication, temperature not specified in the publication
0.028
-
truncated protein, residues 76-679, pH not specified in the publication, temperature not specified in the publication
0.009
-
within a sulfite concentration range of 0.0014-0.3 mM and with a fixed reduced coenzyme F420 concentration of 0.04 mM
0.0122
-
pH 7.0, temperature not specified in the publication
0.012
-
reaction with cytochrome c
reaction with ferricyanide
pH 6.0, temperature not specified in the publication
3.1
-
pH 7.5, 37°C
0.35
-
pH 7.6, 22°C
0.06
-
-
0.01
-

Ki Value (25 results)

top print hide
COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
-
0.0014
-
wild type enzyme, at pH 7.3 and 25°C
0.00031
-
mutant enzyme R301K, at pH 7.3 and 25°C
0.078
-
sulfite resembles the sulfonate part of thiosulfate and might, therefore, block the active site of the enzyme
0.3
-
-
0.005
-
pH 6.0, 80°C
0.005
-
pH 7.0, 25°C
0.19
-
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
11.7
-
pH 8.3, 22°C, inhibition of CO2 hydration activity
37.5
-
pH 8.3, 20°C, inhibition of CO2 hydration activity
24.1
-
pH 8.3, 20°C
1.29
-
pH 7.5, 20°C, inhibition of CO2 hydration reaction
0.008
-
pH 7.5, 20°C, inhibition of CO2 hydration activity
14.9
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
0.43
-
isozyme CA XV
0.0097
-
Co(II)-substituted enzyme, pH and temperature not specified in the publication
1.8
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.33
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
at 20°C and pH 7.5 in 10 mM HEPES buffer
0.01
-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
11.7
-
20°C, pH not specified in the publication, Co2+-substituted enzyme
1.8
-
20°C, pH not specified in the publication
45.1
-

IC50 Value (1 result)

top print hide
COMMENTARY
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
LITERATURE
pH 7.5, 20°C, inhibition of CO2 hydration activity
0.59
-

References & Links

top