Ligand sodium azide

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Basic Ligand Information

Molecular Structure
Picture of sodium azide (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
N3Na
sodium azide
PXIPVTKHYLBLMZ-UHFFFAOYSA-N
Synonyms:
Na-azide, NaN3

Show all pahtways known for Show all pathways known for sodium azide

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (2 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (19 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
10 mM stimulates 2fold
-
1 mM, relative activity 102%
-
activates slightly
-
Co QueD: 110% activity remains after 15 min incubation with 1 mM reagent, Mn QueD = 100% activity remains after 15 min incubation with 1 mM reagent
-
1 mM, 128% of initial activity
-
20 mM concentration 60% activation
-
activation
-
116% activity at 1 mM (pH 7.0)
-
0.1 mM, 37% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
0.1 mM, 37% activation. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
70% stimulation at 10 mM
-
1M, enhanced enzyme activity, only in mutants
-
for D766A mutant only
-
hydrolysis of locust bean gum is enhanced by approximately 1.45fold in poresence of sodium azide
-
accelerates casein digestion
-
1 mM, relative activity 101%
-
10 mM
-
0.01 M, activates
-
activation
-

Inhibitor in Enzyme-catalyzed Reactions (393 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
88% inhibition at 10 mM
-
15% inhibition of the reductive reaction at 5 mM; slight
-
slight inhibition at 2 mM
-
slight inhibition at 10 mM
-
slight inhibition at 1 mM
-
slight inhibition at 1 mM
-
1 mM, complete loss of activity
-
25% inhibition at 1 mM
-
weak
-
0.97 mM, 90% residual activity
-
10 mM, 40% inhibition
-
2 mM, 35% residual activity
-
slightly inhibitory at 1 mM, more than 85% activity remains
-
18.5% inhibition at 1 mM
-
12% inhib ition at 2 mM
-
1 mM, 28.6% residual activity
-
complete inhibition at 1 mM
-
65% inhibition at 1 mM
-
1 mM, 9.1% inhibition
-
no activity
-
25% inhibition at 2 mM; 2 mM, 25% inhibition
-
1 mM, 76% inhibition
-
0.05 mM, complete inhibition of bromoperoxidase-catalase activity
-
slightly destabilizes the enzyme
-
the immobilized enzyme is less sensitive compared to the free enzyme
-
complete inhibition at 0.5 mM
-
1 mM, 90% residual activity
-
slight inhibition
-
40 mM, 46% inhibition of ferredoxinNAP reductase
-
50% inhibition at 2 mM
-
14.6% inhibition at 5 mM
-
5 mM NaN3 inhibits activity by 16%
-
10 mM, 64% loss of activity
-
92% inhibition b
-
1 mM, 90% residual activity
-
100% inhibition
-
53% inhibition at 1.7 mM, 5 min preincubation
-
complete inhibition at 1 mM
-
slight inhibition of dehydrogenase activity
-
1 mM, 10 min at 35C, 17% loss of activity
-
competitive with respect to formate
-
40 mM, 46% inhibition
-
46% inhibition at 40 mM
-
25% inhibition in the presence of 1 mM
-
enzyme b, c and d
-
0.1 mM, 20% residual activity
-
5 mM, 52.4% residual AtraAOX2 activity
-
86% residual activity at 1 mM
-
1 mM, 15% inhibition. 5 mM, 53% inhibition
-
1 mM, 26% inhibition
-
100% inhibition at 50 mM, 11% inhibition at 20 mM
-
0.1 mM, 50% inhibition
-
10% inhibition at 2 mM
-
100 mM, 77% inhibition
-
30% inhibition at 1 mM
-
16 mM, 16% inhibition
-
not inhibitory
-
10 mM, 24% inhibition
-
0.1 mM, complete inhibition
-
1 mM, 60% inhibition
-
1 mM, 16% inhibition
-
10 mM, complete inhibition
-
slight
-
1 mM, 74% residual activity
-
7% inhibition at 10 mM
-
1 mM, 32% loss of activity
-
10 mM, no loss of the activity with ferricyanide, 52% loss of the activity with cytochrome c
-
1 mM, 18% inhibition
-
60% inhibition at 1 mM
-
39% inhibition at 10 mM, 10% at 1 mM
-
22% inhibition at 10 mM, 16% at 1 mM
-
5 mM, 32% inhibition, production of methyl iodide
-
2.5 mM; 40% inhibition
-
2.5 mM, 83% residual activity
-
1 M, about 50% inhibition
-
2 mM, 38% inhibition
-
80% inhibition at 10 mM
-
0.267 mM, 42% inhibition
-
5 mM, 70% inhibition
-
93.6% residual activity at 1 mM
-
at 2 mM, 84% residual activity
-
1 mM: 86%, 10 mM: 84% activity, compared to no addition
-
inhibits the enzyme from digestive gland by 36% at 0.01 mM, no inhibition of the enzyme from nervous ganglia
-
immobilized enzyme
-
slight inhibition at 0.1 mM
-
strong inhibition
-
slight inhibition at 1 mM
-
IFO 3134, slight inhibition
-
34% inhibition at 1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
-
slightly inhibits
-
complete inhibition at 1 mM
-
slight inhibition at 1 mM
-
weak
-
15 mM, 90% inhibition
-
10 mM, 10% residual activity
-
weak
-
1 mM, 14% inhibition
-
100% inhibition of NADH/FMN cofactor system (anaerobic conditions), 40% inhibition of the ascorbate/cysteine/Fe2+ cofactor system under anaerobic conditions
-
26-29% reduced activity at 1 mM
-
10 mM, 18% inhibition
-
10 mM
-
FGK2 complex
-
partial
-

Metals and Ions (11 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, activation of reaction with lactose (0.0125 mM) to 110% of control
-
1 mM, 50% stimulation of menadione reduction
-
30% activation at 1 mM
-
activates
-
effects on kinetics, overview
-
5 mM, complete inhibition. Azide can bind via the Mg2+-binding sites (whether ATP is in the active site or not) and inactivate the enzyme. It is a mixed non-competitive inhibitor because it binds more readily to the enzyme than the enzyme/substrate complex
-
inhibits ATP hydrolysis
-
1 mM, 20% activation
-
activation
-

Enzyme Kinetic Parameters

KM Value (1 result)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
2.3
-
pH 7.6, 25C

Ki Value (35 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.02
-
-
4
-
incompetitive
0.00084
-
at pH 5.6 and 25C
0.08
-
pH 7.5, 24C
2.3
-
pH 7.4, 25 C
3.1
-
pH 7.8, 37C, in the presence of Na+, K+, and Mg2+

IC50 Value (12 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
4.32
-
competitive with 4-methylcatechol or pyrogallol, noncompetitive with catechol as substrate. IC50: 1.31 mM in reaction with 4-methylcatechol, IC50: 10.3 mM in reaction with pyrogallol, IC50: 4.32 mM in reaction with catechol
0.11
-
pH 4.0, 65C
1.529
-
at pH 7.0 and 20C

References & Links

Links to other databases for sodium azide

ChEBI
PubChem
ChEBI
PubChem