Ligand Sulfide

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Basic Ligand Information

Molecular Structure
Picture of Sulfide (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
H2S
Sulfide
Synonyms:
bisulfide, H2S, HS-, hydrogen-sulfide, hydrogen sulfide, hydrogensulfide, hydrosulfide, SH-, SH2, sulphur hydride
Pathway Source
Pathways
BRENDA
cysteine metabolism, hydrogen production, sulfate reduction
KEGG
Carbon metabolism, Cysteine and methionine metabolism, Microbial metabolism in diverse environments, Sulfur metabolism
MetaCyc
4,4'-disulfanediyldibutanoate degradation, assimilatory sulfate reduction I, assimilatory sulfate reduction II, assimilatory sulfate reduction III, assimilatory sulfate reduction IV more


Show all pahtways known for Show all BRENDA pathways known for Sulfide

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (29 results)

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EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
hydrogen sulfide + glutathione + a quinone = S-sulfanylglutathione + a quinol
-
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
acetyl-CoA + hydrogen sulfide = CoA + thioacetate
-
show the reaction diagram
NAD+ + glycine + sulfide = nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 3 H2O
-
show the reaction diagram
O-acetyl-L-serine + sulfide = L-cysteine + acetate
-
show the reaction diagram
O-phospho-L-seryl-tRNACys + sulfide = L-cysteinyl-tRNACys + phosphate
-
show the reaction diagram
hydrogen sulfide + L-aspartate 4-semialdehyde + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = L-homocysteine + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
-
show the reaction diagram
sulfide + tRNA-uridine = tRNA-4-thiouridine
-

In Vivo Product in Enzyme-catalyzed Reactions (38 results)

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EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
sulfur = H2S
-
-
show the reaction diagram
sulfite + 6 ferrocytochrome c + 6 H+ = H2S + 3 H2O + 6 ferricytochrome c
-
-
show the reaction diagram
sulfur + NAD(P)H + H+ = hydrogen sulfide + NAD(P)+
-
-
show the reaction diagram
(sulfide)n+1 + NADPH + H+ = hydrogen sulfide + (sulfide)n + NADP+
-
-
show the reaction diagram
thiosulfate + 2 ferrocytochrome c3 = sulfite + hydrogen sulfide + 2 ferricytochrome c3
-
-
show the reaction diagram
methanethiol + O2 + H2O = formaldehyde + H2S + H2O2
-
-
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
3-mercaptopyruvate + cyanide = H2S + ?
-
-
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
carbonyl sulfide + H2O = CO2 + H2S
-
-
show the reaction diagram
carbonyl sulfide + H2O = hydrogen sulfide + CO2
-
-
show the reaction diagram
D-cysteine + H2O = sulfide + NH3 + pyruvate
-
-
show the reaction diagram
L-cysteine + H2O = sulfide + NH3 + pyruvate
-
show the reaction diagram
D-cysteine + H2O = sulfide + NH3 + pyruvate
-
-
show the reaction diagram
L-cysteine + H2O = sulfide + NH3 + pyruvate
-

Substrate in Enzyme-catalyzed Reactions (152 results)

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EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
sulfide + O2 = sulfur + H2O2
-
show the reaction diagram
sulfite + hydrogen sulfide + menaquinone = thiosulfate + menaquinol
-
show the reaction diagram
hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O = sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
-
show the reaction diagram
acetyl-CoA + hydrogen sulfide = CoA + thioacetate
-
show the reaction diagram
NAD+ + glycine + sulfide = nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 3 H2O
-
show the reaction diagram
O-succinyl-L-homoserine + H2S = L-homocysteine + succinate
-
show the reaction diagram
hydrogen sulfide + L-aspartate 4-semialdehyde + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = L-homocysteine + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
-
show the reaction diagram
sulfide + adenylated-tRNA-uridine(position8) = tRNA-4-thiouridine(position8) + ?
-
show the reaction diagram
3-phospho-L-serine + sulfide = ?
-
show the reaction diagram
L-Seryl-tRNASec + sulfide = ?
-
show the reaction diagram
horse heart cytochrome c + sulfide = ?
-
show the reaction diagram
O-Acetyl-L-serine + H2S = Cysteine + acetate
-
show the reaction diagram
O-acetyl-D-serine + sulfide = D-cysteine + ?
-
show the reaction diagram
3-chloro-D-alanine + H2S = D-cysteine + HCl
-

Product in Enzyme-catalyzed Reactions (200 results)

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EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
H2 + sulfur = H2S
-
-
show the reaction diagram
(sulfide)n+1 + NADPH + H+ = hydrogen sulfide + (sulfide)n + NADP+
-
-
show the reaction diagram
sulfur + reduced benzyl viologen + H+ = sulfide + oxidized benzyl viologen
-
-
show the reaction diagram
thiosulfate + menaquinol = sulfite + hydrogen sulfide + menaquinone
-
-
show the reaction diagram
L-homocysteine + KCN = gamma-cyano-alpha-aminobutyric acid + H2S
-
-
show the reaction diagram
L-cysteine + dithiothreitol = S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + sulfide
-
show the reaction diagram
thiosulfate + glutathione = sulfite + glutathione disulfide + sulfide
-
show the reaction diagram
L-cysteine = L-alanine + sulfide
-
-
show the reaction diagram
carbonyl sulfide + H2O = hydrogen sulfide + CO2
-
-
show the reaction diagram
benzoyl-thiocarbamic acid + H2O = N-benzoyl-Gly + SH2
-
-
show the reaction diagram
D-cysteine + H2O = sulfide + NH3 + pyruvate
-
show the reaction diagram
L-Cys + sulfite = L-cysteate + H2S
-
-
show the reaction diagram
D-cysteine + H2O = sulfide + NH3 + pyruvate
-

Activator in Enzyme-catalyzed Reactions (17 results)

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COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (66 results)

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COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 97% inhibition
-
at high sulfide concentrations, enzymic inhibition is observed above 0.25 mM (20% inhibition at 0.3 mM sulfide)
-
0.1 mM, 10% inhibition
-
sulfide, elemental sulfur, elemental selenium or hydroxylamine required in catalytic amount, inhibition when added over a critical concentration (with the exception of hydroxylamine)
-
substrate analogue, formation of a green complex upon binding
-
1 mM, 10 min, reversible time-dependent inactivation
-
complete loss of activity without previous KCN-treatment
-
partial
-
Na2S
-
reduction of sulfite, nitrite, hydroxylamine by reduced methyl viologen
-
non-competitive inhibition of methyl mercaptan oxidation
-
no inhibition
-
the enzyme activity decreases when the ambient sulfide concentration exceeds 0.3 mM
-
Na2S at 0.5 mM inactivates completely
-
10 mM, 84% inhibition, production of methyl iodide
-
above 200 mM
-
above 107 mM
-
substrate inhibition
-
no inhibition
-
4 mM, 65% inhibition
-
inhibitory effect
-
at concentrations above 30 mM
-
activating at 0.1 mM, inhibitory above 0.3 mM, in human colon cancer cell line HT-29
-
product inhibition, competitive versus both substrates
-
optimal sulfide concentration for 4-thiouridine modification of tRNAPhe is about 50 mM. Higher sulfide concentrations are inhibitory
-
Zn2+ but not Cd2+, Ca2+ or Mg2+ could counteract the inhibitory effect
-
shows low micromolar inhibition against CA XV
carbonic anhydrase XIII
best inhibitor of the Zn(II)-substituted enzyme
best inhibitor
best Can2 anion inhibitor
best anion inhibitors for Zn2+-substituted enzyme are cyanate and hydrogen sulfide
inhibition is fully reversible; low-micromolar levels of sulfide directly inhibit the proton-pumping cytochrome bo oxidase, but not cytochrome bd oxidase
-
1-3 mM, complete inhibition
-
heme-binding inhibitor, noncompetitive vs. O2 and cytochrome c
-

Metals and Ions (47 results)

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COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
7.2 mol labile sulfide per enzyme
14.4 atoms per molecule
24 g acid labile sulfide per 185 g enzyme
7.2 mol labile sulfide per enzyme
10 atoms labile sulfide per mol enzyme
7.2 mol labile sulfide per enzyme
9.1 mol per mol enzyme, iron-sulfur protein
14.4 atoms per molecule
10 atoms labile sulfide per mol enzyme
10.8 mol acid labile sulfur per mol of enzyme
12 atoms acid labile sulfur atoms per mol enzyme
14.4 atoms per molecule
component B contains 1.7 mol and A 6.0 mol of acid-labile sulfide per mol of enzyme
-
iron atoms are coordinated by 4 cysteines and are bridged by a pair of acid-labile sulfur atoms in the 2Fe2S ferredoxins
-
iron-sulfur protein
-
activation, in vitro
-

3D Structure of Enzyme-Ligand-Complex (PDB) (664 results)

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EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (71 results)

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COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
mutant enzyme C160A, at pH 7.0 and 23°C
0.1
-
wild type enzyme, at pH 7.0 and 23°C
6.5
-
solubilized enzyme, at pH 6.8 and 25°C
62
-
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
343
-
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
379
-
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
recombinant enzyme, at pH 7.4 and 47°C
54
-
mutant enzyme H132A, at pH 7.0 and 23°C
1.4
-
mutant enzyme C356S, at pH 7.0 and 23°C
0.1
-
mutant enzyme C198A, at pH 7.0 and 23°C
0.3
-
mutant enzyme C160S, at pH 7.0 and 23°C
0.5
-
mutant enzyme C128S, at pH 7.0 and 23°C
1.6
-
mutant enzyme C128A, at pH 7.0 and 23°C
1
-
pH 7.5, 60°C, membrane-bound wild-type enzyme
0.6
-
enzyme in nanodiscs, at pH 6.8 and 25°C
84
-
cosubstrates sulfite, ubiquinone-1, pH 7.5, 25°C
379
-
cosubstrates sulfide, ubiquinone-1, pH 7.0, 25°C
65
-
cosubstrates cyanide, ubiquinone-1, pH 8.5, 25°C
343
-
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
0.82
-
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
0.62
-
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
1.2
-
pH 7.4, 25°C
74
-
with sulfite as acceptor, at pH 7.4 and 37°C
113
-
solubilized enzyme, at pH 6.8 and 25°C
62
-
with cysteine as acceptor, at pH 7.4 and 37°C
92
-
enzyme in nanodiscs, at pH 6.8 and 25°C
84
-
with glutathione as acceptor, at pH 7.4 and 37°C
94
-
with homocysteine as acceptor, at pH 7.4 and 37°C
74
-
at pH 7.4 and 37°C
373
-
pH 7.0, 30°C
0.0381
-
sulfhydrylation of O-acetyl-L-serine
202
-
wild-type, pH 7.0, 25°C
2170
-
wild-type, pH 8.0, 30°C
12
-
pH 7.5, 23°C
32.65
-
mutant T74S, pH 7.0, 25°C
1700
-
pH 7.0, 40°C
2.43
-
pH 6.5, 50°C
32.99
-
mutant Y97M, pH 8.0, 30°C
22
-
mutant V74T, pH 8.0, 30°C
26
-
at pH 7.4 and 25°C
6.3
-
mutant H157N, pH 7.0, 25°C
1990
-
mutant H157Q, pH 7.0, 25°C
1780
-
mutant N77A, pH 7.0, 25°C
155
-
mutant N77D, pH 7.0, 25°C
0.73
-
mutant Q147A, pH 7.0, 25°C
12.5
-
mutant Q147S, pH 7.0, 25°C
0.22
-
mutant S121A, pH 8.0, 30°C
15
-
mutant S121M, pH 8.0, 30°C
44
-
mutant S269A, pH 7.0, 25°C
29.5
-
mutant S269T, pH 7.0, 25°C
929
-
mutant S75A, pH 7.0, 25°C
20.2
-
mutant S75N, pH 7.0, 25°C
1.45
-
mutant Y97F, pH 8.0, 30°C
10
-
mutant T78S, pH 7.0, 25°C
370
-
mutant T78A, pH 7.0, 25°C
537
-
30°C, pH 8.0
12
-
mutant S75T, pH 7.0, 25°C
82.7
-
mutant T182A, pH 7.0, 25°C
1600
-
mutant T182S, pH 7.0, 25°C
1690
-
mutant T185A, pH 7.0, 25°C
1.44
-
mutant T74A, pH 7.0, 25°C
0.42
-
mutant T185S, pH 7.0, 25°C
5.57
-
pH 7.5, 25°C
96.65
-
pH 7.5, 80°C, wild-type enzyme, with O-phospho-L-serine
730
-
pH 7.5, 80°C, mutant F225A, with O-phospho-L-serine
130
-
pH 7.5, 80°C, wild-type enzyme, with O-acetyl-L-serine
33
-
cosubstrate L-serine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
0.78
-
cosubstrate L-serine, pH 7.4, 37°C
0.35
-
pH 8.5, 31°C

KM Value (169 results)

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COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
at pH 6.0 and 30°C
0.0023
-
in 10 mM Tris-HCl buffer, pH 8.5, at 20°C
0.0125
-
pH and temperature not specified in the publication
0.0017
-
-
0.06
-
20 mM Tris-HCl, pH 8.0, at 22°C
0.23
-
apparent value, at pH 7.0, temperature not specified in the publication
0.042
-
cosubstrates cyanide, ubiquinone-1, pH 8.5, 25°C
0.0109
-
cosubstrates sulfide, ubiquinone-1, pH 7.0, 25°C
0.315
-
cosubstrates sulfite, ubiquinone-1, pH 7.5, 25°C
0.013
-
enzyme in nanodiscs, at pH 6.8 and 25°C
0.23
-
in 10 mM bis-Tris-HCl, pH 6.5, temperature not specified in the publication
0.002
-
in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22°C
0.008
-
in 10 mM potassium HEPES (pH 7.4), 10 mM MgCl2, 10 mM KCl, temperature not specified in the publication
0.02
-
in 50 mM 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)propane-1,3-diol (pH 6.5), temperature not specified in the publication
0.0028
-
in 50 mM Bis-Tris (pH 6.5), temperature not specified in the publication
0.026
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
0.011
-
in 50 mM Tris-HCl, pH 7.4, 40°C
0.00594
-
Km above 0.4 mM, mutant enzyme V300D, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.4
-
mutant enzyme C128A, at pH 7.0 and 23°C
0.0056
-
mutant enzyme C128S, at pH 7.0 and 23°C
0.00553
-
mutant enzyme H131A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.011
-
mutant enzyme H132A, at pH 7.0 and 23°C
0.005
-
mutant enzyme H196A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.015
-
pH 7.4, 25°C
0.32
-
pH 7.4, temperature not specified in the publication
0.00594
-
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
0.077
-
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
0.073
-
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
0.046
-
pH 7.5, 60°C, membrane-bound wild-type enzyme
0.077
-
pH 7.5, 60°C, wild-type enzyme
0.077
-
recombinant enzyme, at pH 7.4 and 47°C
1.95
-
solubilized enzyme, at pH 6.8 and 25°C
0.35
-
wild type enzyme, at pH 7.0 and 23°C
0.00297
-
wild type enzyme, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.005
-
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
0.0109
-
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
0.013
-
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
0.315
-
at pH 7.4 and 25°C
at pH 7.4 and 37°C
0.32
-
at pH 7.8 and 25°C
2
-
enzyme in nanodiscs, at pH 6.8 and 25°C
0.23
-
solubilized enzyme, at pH 6.8 and 25°C
0.35
-
with cysteine as acceptor, at pH 7.4 and 37°C
0.005
-
with glutathione as acceptor, at pH 7.4 and 37°C
0.01
-
with homocysteine as acceptor, at pH 7.4 and 37°C
0.007
-
with sulfite as acceptor, at pH 7.4 and 37°C
0.13
-
with ubiquinone as cosubstrate, at pH 8.5 and 37°C
0.043
-
-
0.064
-
in 20 mM MES (pH 7.0), at 30°C
12.24
-
pH 7.0, 30°C
9.9
-
pH 7.0, 30°C, purified recombinant enzyme
12.24
-
pH and temperature not specified in the publication
0.6
-
30°C, pH 8.0
0.12
-
37°C, pH 7.8, cosubstrate: O-acetyl-L-Ser
0.8
-
37°C, pH 7.8, cosubstrate: O-phosphoserine
0.029
-
37°C, pH 9.0
0.031
-
40°C
0.5
-
at pH 7.4 and 25°C
0.16
-
isoenzyme 1 and 2
0.6
-
isoform A, pH 7.5, 25°C, Hill equation, Hill coefficient 0.81
6.4
-
isoform A, pH 7.5, 25°C, Michaelis-Menten kinetics
5.6
-
isoform B, pH 7.5, 25°C, Hill equation, Hill coefficient 0.75
3.2
-
isoform B, pH 7.5, 25°C, Michaelis-Menten kinetics
3
-
isoform C, pH 7.5, 25°C, Hill equation, Hill coefficient 1.05
4.6
-
isoform C, pH 7.5, 25°C, Michaelis-Menten kinetics
4.7
-
less than
0.1
-
mutant H157N, pH 7.0, 25°C
0.4
-
mutant H157Q, pH 7.0, 25°C
0.3
-
mutant N77A, pH 7.0, 25°C
0.23
-
mutant N77D, pH 7.0, 25°C
0.18
-
mutant Q147A, pH 7.0, 25°C
1.7
-
mutant Q147S, pH 7.0, 25°C
0.27
-
mutant S121A, pH 8.0, 30°C
0.095
-
mutant S121M, pH 8.0, 30°C
0.2
-
mutant S269A, pH 7.0, 25°C
0.54
-
mutant S269T, pH 7.0, 25°C
1.6
-
mutant S75A, pH 7.0, 25°C
4.6
-
mutant S75N, pH 7.0, 25°C
5.7
-
mutant S75T, pH 7.0, 25°C
0.21
-
mutant T182A, pH 7.0, 25°C
0.39
-
mutant T182S, pH 7.0, 25°C
0.22
-
mutant T185A, pH 7.0, 25°C
0.22
-
mutant T185S, pH 7.0, 25°C
0.36
-
mutant T74A, pH 7.0, 25°C
3.9
-
mutant T74S, pH 7.0, 25°C
3.2
-
mutant T78A, pH 7.0, 25°C
0.44
-
mutant T78S, pH 7.0, 25°C
0.3
-
mutant V74T, pH 8.0, 30°C
0.14
-
mutant Y97F, pH 8.0, 30°C
0.073
-
mutant Y97M, pH 8.0, 30°C
0.084
-
pH 6.5, 50°C
0.252
-
pH 6.8, 37°C
0.59
-
pH 7.0, 25°C, recombinant free enzyme
0.37
-
pH 7.0, 40°C
0.06
-
pH 7.4, 30°C
0.5
-
pH 7.4, 37°C
6.7
-
pH 7.4, 37°C, enzyme 1
0.4
-
pH 7.4, 37°C, isoenzyme 2
1.6
-
pH 7.5, 22°C, recombinant enzyme, Lineweaver-Burke model
1.46
-
pH 7.5, 22°C, recombinant enzymem, Michaelis-Menten model
1.85
-
pH 7.5, 23°C
0.078
-
pH 7.5, 25°C
pH 7.5, 25°C, chloroplast enzyme
0.25
-
pH 7.5, 25°C, enzyme bound to serine acetyltransferase
0.013
-
pH 7.5, 25°C, free enzyme
0.006
-
pH 7.5, 25°C, recombinant complex-bound enzyme
0.55
-
pH 7.5, 37°C
pH 7.5, 37°C, isoenzyme 1 and 2
0.8
-
pH 7.5, 50°C
0.75
-
pH 7.5, 50°C, isoenzyme 1 and 2
5.2
-
pH 7.5, enzyme form PCS-1
1.57
-
pH 7.5, enzyme form PCS-2
0.998
-
pH 7.8, 35° C
0.24
-
pH 7.8, 35°C
pH 7.8, 35°C, isoenzyme 2
0.038
-
pH 7.8, 50°C
0.05
-
pH 8.0, 25°, isoenzyme 1'
0.66
-
pH 8.0, 25°C, isoenzyme 1
0.55
-
pH 8.0, 25°C, isoenzyme 2
1.25
-
pH 8.0, 25°C, isoenzyme 3
2.5
-
pH 8.0, 30°C
pH 8.0, 30°C, isoenzyme 1
0.033
-
wild-type, pH 7.0, 25°C
0.22
-
wild-type, pH 8.0, 30°C
0.12
-
pH 7.3, 30°C, gamma-replacement reaction
3
-
pH 7.5, 25°C
0.4
-
60°C, O-acetyl-L-serine sulfhydrylation reaction
0.25
-
60°C, O-phospho-L-serine sulfhydrylation reaction
5
-
85°C, O-phospho-L-serine sulfhydrylation reaction
12.5
-
below, pH 6.7
0.2
-
pH 7.5, 80°C, mutant F225A, with O-phospho-L-serine
1.6
-
pH 7.5, 80°C, wild-type enzyme, with O-acetyl-L-serine
0.39
-
pH 7.5, 80°C, wild-type enzyme, with O-phospho-L-serine
3.8
-
pH 7.6, 60°C, with O-acetyl-L-serine
0.25
-
pH 7.6, 60°C, with O-phospho-L-serine
5
-
pH 7.6, 85°C, with O-phospho-L-serine
12.5
-
20°C, pH 9.2
8.8
-
pH 7.3, 37°C
1
-
cosubstrate L-serine, pH 7.4, 37°C
5.02
-
cosubstrate L-serine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
4.7
-
pH 8.5
9.51
-
pH 8.5, 31°C
-
46
-

Ki Value (25 results)

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COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
pH 7.5, 30°C
-
0.09
-
pH 7.5, 22°C
1.35
-
pH 8
0.025
-
pH 8.0, 30°C
-
0.076
-
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
0.05
-
pH 8.3, 22°C, inhibition of CO2 hydration activity
4.8
-
pH 8.3, 20°C, inhibition of CO2 hydration activity
8.4
-
pH 8.3, 20°C
pH 7.5, 20°C, inhibition of CO2 hydration activity
20.4
-
pH 7.5, 20°C
0.00009
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
3.94
-
isozyme CA XV
0.0092
-
Co(II)-substituted enzyme, pH and temperature not specified in the publication
2
-
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
0.41
-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
0.05
-
20°C, pH not specified in the publication, Co2+-substituted enzyme
2
-
20°C, pH not specified in the publication
0.7
-

IC50 Value (3 results)

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COMMENTARY
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
LITERATURE
pH 7.5, 20°C, inhibition of CO2 hydration activity
1
-
cytochrome bo oxidase, at pH 7.0 and 25°C
0.005
-
pH 7.4, 25°C
0.0011
-

References & Links

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