Ligand potassium cyanide

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Basic Ligand Information

Molecular Structure
Picture of potassium cyanide (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
CKN
potassium cyanide
NNFCIKHAZHQZJG-UHFFFAOYSA-N
Synonyms:
KCN

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (12 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
potassium cyanide + H2O = potassium carbonate + NH3
show the reaction diagram
-
potassium cyanide + H2O = ?
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (15 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
0.1 mM, 37% increase
-
1 mM, relative activity 101%
-
18% activation at 0.5 mM
-
2fold activation at 1-10 mM
-
slight
-
activation at 6.7 mM up to 10 mM when both alternative pathways to oxygen are inhibited
-
enhances the lysine oxidase activity (177% activity at 1 mM (pH 5.5))
-
slight stimulatuion after 30 min of incubation
-
slight activation at 1 mM
-
without cAMP stimulation, KCN treatment increases CFTR Cl- conductance by 1.95fold, whereas after cAMP stimulation KCN treatment increases conductance by 13.7fold
-

Inhibitor in Enzyme-catalyzed Reactions (381 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 41% inhibition
-
25% inhibition of the reductive reaction at 2.5 mM; slight
-
slight inhibition at 2 mM
-
complete inhibition at 1 mM
-
73% inhibition at 1 mM
-
15% inhibition at 1 mM
-
complete inhibition at 10 mM
-
55% inhibition at 2 mM
-
weak inhibition
-
65.2% inhibition at 1 mM, complete inhibition at 10 mM
-
1 mM, 12.7% residual activity
-
complete inhibition
-
complete inhibition at 1 mM
-
1 mM inhibits
-
28% residual activity at 100 mM
-
2 mM, 90% inhibition; 90% inhibition at 2 mM
-
70% inhibition at 5 mM
-
0.05 mM, complete inhibition of bromoperoxidase-catalase activity
-
0.01 mM, 50% inhibition
-
0.1 mM, 82% inhibition
-
60-70% inhibition at 10 mM
-
85% inhibition at 0.1 mM
-
largely irreversible losses
-
; strongly
-
little or no effect
-
40% inhibition at 2 mM
-
1 mM, 52% inhibition
-
70% inhibition at 10 mM
-
78.7% inhibition at 0.5 mM
-
5 mM, 80% residual activity
-
10 mM, 21% loss of activity
-
30 mM, 21% inhibition
-
slight inhibitor
-
pMMO
-
1 mM, loss of most of the desaturase activity
-
83% inhibition by 1 mM, 95% inhibition by 5 mM
-
5 mM, 42% loss of activity
-
5 mM, 63% inhibition
-
25% inhibition
-
60% inhibition
-
0.1 mM, 20% inhibition
-
isozymes A and C
-
10-20% inhibition at 1 mM
-
1 mM causes 33% inhibition
-
13% residual activity at 1 mM
-
25% inhibition at 10 mM
-
41% activity retained at 5 mM concentration
-
20 mM concentration 25% inhibition
-
complete inhibition at 20 mM after 1 h incubation at room temperature
-
5 mM, 64% inhibition
-
1 mM, 26% inhibition
-
complete inhibition of orotate reductase reaction
-
protection by FAD
-
inhibition with all cofactors except the methyl viologen dependent activity
-
1 mM, 24% inhibition
-
89% inhibition at 20 mM
-
50 mM, strong inhibition of isozymes 1-3
-
0.1 mM, 50% inhibition
-
1 mM, 43% inhibition
-
47% inhibition at 7.1 mM
-
remarkable inhibition at 1 mM, inhibition is only slight with 2,6-dichlorophenol-indophenol electron acceptor but higher when indophenol is used
-
slight inhibition
-
0.01 M, 10% inhibition
-
1.3 mM, about 40% inhibition
-
20% inhibition at 1 mM
-
very strong inhibition
-
1 mM
-
10 mM, 36% inhibition
-
0.1 mM, complete inhibition
-
although 1 mM KCN completely inhibits hydroxylamine reduction, it does not inhibit the reduction of K3Fe(CN)6 and only decreases the rate of cytochrome c reduction by 12%
-
0.1 mM, 84% inhibition; 1 mM, 100%
-
1 mM, complete inhibition
-
complete inhibition at 1 mM
-
0.1 mM
-
2 mM, complete inhibition after 10 min
-
1 mM, complete inhibition
-
88% inhibition at 100 mM, 44% inhibition at 10 mM
-
74% inhibition at 100 mM, but 33% activation at 10 mM
-
1 mM, 26% inhibition
-
weak
-
58% inhibition at 0.1 M
-
13% inhibition at 0.1 mM
-
15.6% inhibition by 1 mM
-
10 mM, almost complete inhibition
-
100 mM, complete
-
weak inhibition
-
1 mM, 38% inhibition
-
1 mM, 93% inhibition, pyridoxal 5'-phosphate protects
-
1 mM: 22% inhibition
-
complete inhibition
-
irreversible inhibitor
-
1 mM, 38% remaining activity for CAT 1, less efficient inhibitor for CAT-IIA and CAT-IIB
-
little effect
-
62% inhibition at 1 mM
-
62% inhibition of the catalytic fragment of CNP1
-
10 mM, 23% residual activity
-
slight
-
25 mM, 70% inhibition
-
10 mM, 84% inhibition
-
similar effect as with imidazole, hemoglobin hydrolysis inhibited, cleavage of small synthetic peptide and ester substrates enhanced
-
10 mM, 42% inhibition
-
slight inhibition at 8 mM
-
10 mM, 12% loss of activity
-
10 mM, 12% inhibition
-
KCN inhibits dihydropterin deaminase activity strongly 98.6% inhibition at 10 mM whereas it has almost no inhibitory effect on guanine deaminase activity at the same concentration
-
weak
-
strong inhibitor
-
non-competitive
-
1 mM, 68% inhibition
-
1 mM, 26% inhibition
-
20% inhibition at 1 mM, 40% inhibition at 5-10 mM
-
10 mM almost complete inhibition
-
22% inhibition at 1 mM
-
19% residual activity at 1 mM
-
1 mM, 32% inhibition
-
1 mM, 76% inhibition
-

Metals and Ions (10 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activates
-
raises dehydrogenase activity of freshly prepared kidney extracts
-
1 mM, increase to 125% of the activity
-
74% inhibition at 100 mM, but 33% activation at 10 mM
-
slight stimulation
-
slight activation of cyclic phosphodiesterase
-
10 mM, 82% inhibition
-
activates
-
activates at 0.001-0.1 mM, inhibits at 1-10 mM
-

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (2 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE

KM Value (8 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
20
-
pH 9, 37°C, with dithioerythritol as second substrate
0.75
-
-
0.75
-
pH 7.0, 37°C, partially purified enzyme

Ki Value (20 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
7.5
-
pH 8.4, 80°C
0.005
-
-
2.6
-
-

IC50 Value (7 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.3
-
at 37°C
0.21
-
-
0.0064
-
in 25 mM potassium phosphate (pH 7.5), at 30°C

References & Links

Links to other databases for potassium cyanide

ChEBI
PubChem
ChEBI
PubChem