3.5.4.6: AMP deaminase
This is an abbreviated version!
For detailed information about AMP deaminase, go to the full flat file.
Word Map on EC 3.5.4.6
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3.5.4.6
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purine
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imp
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deamination
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inosine
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ammonia
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nucleoside
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5'-nucleotidase
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hypoxanthine
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creatine
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phosphorylase
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myopathy
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coformycin
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mcardle
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fatigue
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phosphofructokinase
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myalgia
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forearm
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phosphocellulose
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cramp
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athlete
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hypoxanthine-guanine
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phosphocreatine
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fast-twitch
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deaminases
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orthophosphate
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nh3
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rhabdomyolysis
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myokinase
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slow-twitch
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half-saturation
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myoglobinuria
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ergometer
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myophosphorylase
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2\'-deoxycoformycin
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hgprt
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medicine
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biotechnology
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food industry
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analysis
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synthesis
- 3.5.4.6
- purine
- imp
-
deamination
- inosine
- ammonia
- nucleoside
- 5'-nucleotidase
- hypoxanthine
- creatine
- phosphorylase
- myopathy
- coformycin
- mcardle
-
fatigue
-
phosphofructokinase
- myalgia
- forearm
-
phosphocellulose
- cramp
-
athlete
-
hypoxanthine-guanine
- phosphocreatine
-
fast-twitch
- deaminases
- orthophosphate
- nh3
- rhabdomyolysis
- myokinase
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slow-twitch
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half-saturation
- myoglobinuria
-
ergometer
- myophosphorylase
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2\'-deoxycoformycin
- hgprt
- medicine
- biotechnology
- food industry
- analysis
- synthesis
Reaction
Synonyms
5'-adenosine monophosphate deaminase, 5'-adenylic acid deaminase, 5-adenylate deaminase, 5-adenylic acid deaminase, 5-AMP aminohydrolase, 5-AMP deaminase, adenosine 5-monophosphate deaminase, adenosine 5-phosphate aminohydrolase, adenosine 5-phosphate deaminase, adenosine monophosphate deaminase, adenosine monophosphate deaminase 3, adenosine monophosphate deaminase-1, adenosine-5'-monophosphate deaminase, adenyl deaminase, adenylate aminohydrolase, adenylate deaminase, adenylate desaminase, adenylic acid deaminase, adenylic deaminase, AMP aminase, AMP deaminase, AMP deaminase 3, AMP deaminase H-type, AMP deaminase isoform E, AMP deaminase type 3, AMP deaminase1, AMP-aminohydrolase, AMP-deaminase, AmpD, AMPD1, AMPD2, AMPD3, AMPDA, deaminase, adenylate, embryonic factor 1, EMBRYONIC FACTOR1, Erythrocyte AMP deaminase, FAC1, Heart-type AMPD, muscle AMP deaminase, Myoadenylate deaminase
ECTree
3.5.4.6 AMP deaminaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 3.5.4.6 - AMP deaminase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(S)-2-(4-bromo-biphenyl-4-sulfonyl)amino-3-methyl butyric acid
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i.e. PD166793
1,3,4,6,7,8-hexahydro-4,6,6,7,8,8-hexamethyl-cyclopenta-gamma-2-benzopyran
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IC50: 0.0003 mM
1-(5,6,7,8-tetrahydro)3,5,5,6,8,8-hexamethyl-2-naphthalenyl-ethanone
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IC50: 0.0003 mM
1-bromo-4-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
3-[2-(3-carboxy-4-bromo-5,6,7,8-tetrahydronaphthyl)ethyl]-3,6,7,8-tetrahydroimidazo[4,5-d][1,3]diazepin-8-ol
4-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
5,5-dithio-bis(2-nitrobenzoic acid)
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reaction with thiol groups, leads to a decrease of 20-30% in Vmax
H2O2
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treatment with 0.1 mM H2O2 reduces activity by half after about 50 min, 50% of activity is lost in about 25 min when AMPD is incubated with both iron and H2O2
IMP
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uniquely inhibits only the bound (phosphorylated) enzyme from muscle of frozen frogs
N-(2,3,4,6-tetra-O-acetyl-beta-D-glucopyranosyl)pyridinium bromide
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IC50: 0.05 mM
N-(2,3,4,6-tetra-O-acetyl-beta-D-glucopyranosyl)trimethylammonium bromide
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IC50: 0.5 mM
purine riboside
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prolonged exposure (60 min) to purine riboside results in AMPD inhibition
trinitrobenzene sulfonic acid
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regulatory function on activity and inhibition by other compounds, e.g. ATP, overview
additional information
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incubation with 0.005 mM FeSO4 does not affect AMPD activity
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1-bromo-4-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
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1-bromo-4-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
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3-[2-(3-carboxy-4-bromo-5,6,7,8-tetrahydronaphthyl)ethyl]-3,6,7,8-tetrahydroimidazo[4,5-d][1,3]diazepin-8-ol
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specific inhibitor
3-[2-(3-carboxy-4-bromo-5,6,7,8-tetrahydronaphthyl)ethyl]-3,6,7,8-tetrahydroimidazo[4,5-d][1,3]diazepin-8-ol
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specific inhibitor
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
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3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
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good inhibitor of isozyme AMPD3
3-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]benzoic acid
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3-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]benzoic acid
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4-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
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4-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
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ATP
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connection between the operation of the hypothesized anionic activating site, responsible for positive homotropic cooperativity, and the inhibition exerted by anionic compounds that compete for the same site, among them ATP is most efficient, no inhibition of the trinitrobenzene sulfonic acid-desensitized enzyme
ATP
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at pH 5.9 in the absence of fluoride, ATP exerts a biphasic effect; less than 0.003 mM ATP act as an inhibitor, whereas increasing ATP concentrations above 0.003 mM reverse the inhibition
fluoride
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over the pH range 5.9-7.5 fluoride ion acts as pure uncompetitive inhibitor of AMPD, with the Ki increasing from 1 to 30 mM
K+
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inhibitory at concentrations above 300 mM, at 500 mM 62% of initial activities is left
K+
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very weak inhibitor of free AMPD, but shows stronger effect on bound AMPD
Na+
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inhibitory at concentrations above 250 mM, at 500 mM 46% of initial activities is left
Na+
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very weak inhibitor of free AMPD, but shows stronger effect on bound AMPD
phosphate
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competitive inhibitor of the term placenta enzyme, AMP-deaminase from preterm placenta is not inhibited by physiological concentrations of orthophosphate at low substrate concentration range in contrast to the enzyme from the term organ
phosphate
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competitive inhibitor, stabilizing the tetrameric enzyme structure
