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(S)-2-(4-bromo-biphenyl-4-sulfonyl)amino-3-methyl butyric acid
-
i.e. PD166793
1,3,4,6,7,8-hexahydro-4,6,6,7,8,8-hexamethyl-cyclopenta-gamma-2-benzopyran
-
IC50: 0.0003 mM
1-(5,6,7,8-tetrahydro)3,5,5,6,8,8-hexamethyl-2-naphthalenyl-ethanone
-
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
1-n-butyl-3-methylimidazolium chloride
-
IC50: 0.01 mM
1-n-butyl-3-methylimidazolium p-tosylate
-
IC50: 0.01 mM
1-n-butyl-3-methylimidazolium tetrafluoroborate
-
IC50: 0.005 mM
1-n-butyl-3-methylimidazolium tetrafluorophosphate
-
IC50: 0.005 mM
1-t-butyl-3,5-dimethyl-2,4,6-trinitrobenzene
-
IC50: 0.0003 mM
2'-AMP
-
in the absence of ATP
2,3-diphosphoglyceric acid
-
ATP counteracts inhibition
3'-AMP
-
in the absence of ATP
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
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
3-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]benzoic acid
3-[2-(imidazo[2,1-f][1,2,4]triazin-7-yl)ethyl]benzoic acid
4-acetyl-1-t-butyl-3,5-dimethyl-2,6-dinitrobenzene
-
IC50: 0.0005 mM
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)
-
reaction with thiol groups, leads to a decrease of 20-30% in Vmax
Ba2+
-
1 mM, about 20% decrease in activity
Co2+
-
1 mM, about 15% decrease in activity
deaminoformycin
-
0.0003 mM, strong inhibitor
deaminoformycin 5'-monophosphate
-
potent inhibitor
Fe2+
-
1 mM, about 50% decrease in activity
H2O2
-
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
-
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
-
IC50: 0.05 mM
N-(2,3,4,6-tetra-O-acetyl-beta-D-glucopyranosyl)trimethylammonium bromide
-
IC50: 0.5 mM
p-hydroxymercuribenzoate
-
-
phenylmethane-sulfonylfluoride
-
-
purine riboside
-
prolonged exposure (60 min) to purine riboside results in AMPD inhibition
Tannic acid
-
above 0.004 mM, complete inactivation at 0.05 mM
trinitrobenzene sulfonic acid
-
regulatory function on activity and inhibition by other compounds, e.g. ATP, overview
additional information
-
incubation with 0.005 mM FeSO4 does not affect AMPD activity
-
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
-
-
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
-
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
-
specific inhibitor
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
-
-
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
-
good inhibitor of isozyme AMPD3
3-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]benzoic acid
-
-
3-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]benzoic acid
-
-
3-[2-(imidazo[2,1-f][1,2,4]triazin-7-yl)ethyl]benzoic acid
-
-
3-[2-(imidazo[2,1-f][1,2,4]triazin-7-yl)ethyl]benzoic acid
-
-
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
-
-
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'-IMP
-
in the absence of ATP
Al3+
-
1 mM, about 80% decrease in activity
Al3+
-
5 mM, about 35% loss of activity
ATP
-
diethyl pyrocarbonate desensitizes inhibition
ATP
-
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
-
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
Ca2+
-
25% inhibition at 10 mM
Ca2+
-
at 10 mM Ca2+ inhibition of AMPD is 28%
coformycin
-
-
coformycin 5'-phosphate
-
coformycin 5'-phosphate
-
extremely potent AMPD inhibitor
coformycin 5'-phosphate
-
extremely potent AMPD inhibitor
Cu2+
-
1 mM, about 70% decrease in activity
Cu2+
-
5 mM, about 55% loss of activity
Cu2+
-
0.005 mM, about 50% inhibition
EDTA
-
-
F-
-
-
Fe3+
-
1 mM, about 45% decrease in activity
Fe3+
-
5 mM, 72.7% loss of activity
fluoride
-
inhibits AMPD by about 66% at 8 mM
fluoride
-
8 mM fluoride reduce AMPD activity by 54%
fluoride
-
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
GTP
-
-
GTP
-
very strong inhibitor
GTP
-
diethyl pyrocarbonate desensitizes inhibition
GTP
-
wild-type and trinitrobenzene sulfonic acid-desensitized enzyme
iodoacetate
-
not
K+
-
inhibitory at concentrations higher than 80 mM
K+
-
inhibitory at concentrations above 300 mM, at 500 mM 62% of initial activities is left
K+
-
very weak inhibitor of free AMPD, but shows stronger effect on bound AMPD
Mg2+
-
15% inhibition at 10 mM
Mg2+
-
at 10 mM Mg2+ inhibition of AMPD is 13%
Na+
-
inhibitory at concentrations higher than 80 mM
Na+
-
inhibitory at concentrations above 250 mM, at 500 mM 46% of initial activities is left
Na+
-
very weak inhibitor of free AMPD, but shows stronger effect on bound AMPD
Ni2+
-
1 mM, about 20% decrease in activity
phosphate
-
inhibits AMPD by about 66% at 8 mM
phosphate
-
10 mM phosphate lower activity by 39%
phosphate
-
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
-
competitive inhibitor, stabilizing the tetrameric enzyme structure
Zn2+
-
1 mM, about 50% decrease in activity
Zn2+
-
5 mM, about 59.2% loss of activity
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0.0003
1,3,4,6,7,8-hexahydro-4,6,6,7,8,8-hexamethyl-cyclopenta-gamma-2-benzopyran
Rattus norvegicus
-
IC50: 0.0003 mM
0.0003
1-(5,6,7,8-tetrahydro)3,5,5,6,8,8-hexamethyl-2-naphthalenyl-ethanone
Rattus norvegicus
-
IC50: 0.0003 mM
0.01
1-n-butyl-3-methylimidazolium chloride
Rattus norvegicus
-
IC50: 0.01 mM
0.01
1-n-butyl-3-methylimidazolium p-tosylate
Rattus norvegicus
-
IC50: 0.01 mM
0.005
1-n-butyl-3-methylimidazolium tetrafluoroborate
Rattus norvegicus
-
IC50: 0.005 mM
0.005
1-n-butyl-3-methylimidazolium tetrafluorophosphate
Rattus norvegicus
-
IC50: 0.005 mM
0.0003
1-t-butyl-3,5-dimethyl-2,4,6-trinitrobenzene
Rattus norvegicus
-
IC50: 0.0003 mM
0.5
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
Rattus norvegicus
-
-
0.0009 - 0.2
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
0.1 - 1.4
3-[2-(imidazo[2,1-f][1,2,4]triazin-7-yl)ethyl]benzoic acid
0.0005
4-acetyl-1-t-butyl-3,5-dimethyl-2,6-dinitrobenzene
Rattus norvegicus
-
IC50: 0.0005 mM
0.23
IMP
Lithobates sylvaticus
-
myosin-bound AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25°C
0.05
N-(2,3,4,6-tetra-O-acetyl-beta-D-glucopyranosyl)pyridinium bromide
Rattus norvegicus
-
IC50: 0.05 mM
0.5
N-(2,3,4,6-tetra-O-acetyl-beta-D-glucopyranosyl)trimethylammonium bromide
Rattus norvegicus
-
IC50: 0.5 mM
254
NH3
Lithobates sylvaticus
-
free AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25°C
0.0009
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
Homo sapiens
-
isozyme AMPD3, pH and temperature not specified in the publication
0.0023
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
Homo sapiens
-
isozyme AMPD2, pH and temperature not specified in the publication
0.0057
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
Homo sapiens
-
isozyme AMPD1, pH and temperature not specified in the publication
0.2
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
Arabidopsis thaliana
-
pH and temperature not specified in the publication
0.1
3-[2-(imidazo[2,1-f][1,2,4]triazin-7-yl)ethyl]benzoic acid
Homo sapiens
-
isozyme AMPD2, pH and temperature not specified in the publication
0.31
3-[2-(imidazo[2,1-f][1,2,4]triazin-7-yl)ethyl]benzoic acid
Homo sapiens
-
isozyme AMPD1, pH and temperature not specified in the publication
0.37
3-[2-(imidazo[2,1-f][1,2,4]triazin-7-yl)ethyl]benzoic acid
Homo sapiens
-
isozyme AMPD3, pH and temperature not specified in the publication
1.4
3-[2-(imidazo[2,1-f][1,2,4]triazin-7-yl)ethyl]benzoic acid
Arabidopsis thaliana
-
pH and temperature not specified in the publication
0.08
GTP
Lithobates sylvaticus
-
free AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25°C
0.1
GTP
Lithobates sylvaticus
-
myosin-bound AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25°C
162
K+
Lithobates sylvaticus
-
myosin-bound AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25°C
702
K+
Lithobates sylvaticus
-
free AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25°C
133
Na+
Lithobates sylvaticus
-
myosin-bound AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25°C
824
Na+
Lithobates sylvaticus
-
free AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25°C
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Lee, Y.
5'-Adenylic acid deaminase. I. Isolation of the crystalline enzyme from rabbit skeletal muscle
J. Biol. Chem.
227
987-992
1957
Oryctolagus cuniculus
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Lee, Y.
5'-Adenylic acid deaminase. II. Homogeneity and physiochemical properties
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993-998
1957
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5'-Adenylic acid deaminase. III. Properties and kinetic studies
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1957
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Mendicino, J.; Muntz, J.A.
The activating effect of adenosine triphosphate on brain adenylic deaminase
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Canis lupus familiaris
-
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Turner, D.H.; Turner, J.F.
Adenylic deaminase of pea seeds
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79
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Purification and regulatory properties of AMP deaminase from chicken erythrocytes
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The kinetic properties of adenylate deaminase from human erythrocytes
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1978
Homo sapiens
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Human erythrocyte 5-AMP aminohydrolase. Purification and characterization
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253
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1978
Homo sapiens
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Purification, subunit structure, and amino acid composition of avian erythrocyte adenosine monophosphate deaminase
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17
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Gallus gallus
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Nathans, G.R.; Chang, D.; Deuel, T.F.
AMP deaminase from human erythrocytes
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1979
Homo sapiens
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Yoshino, M.; Murakami, K.; Tsushima, K.
AMP deaminase from bakers yeast. Purification and some regulatory properties
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AMPdeaminase from bakers yeast. Kinetic and molecular properties
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AMP deaminase from spinach leaf. Purification and some regulatory properties
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99
331-338
1980
Spinacia oleracea
-
brenda
Stelmach, H.; Jarosewicz, L.
Pig thyroid AMP deaminase purification and some properties
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101
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1981
Sus scrofa
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Ogasawara, N.; Goto, H.; Yamada, Y.; Watanabe, T.; Asano, T.
AMP deaminase isozymes in human tissues
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1982
Homo sapiens
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AMP-deaminase from human skeletal muscle. Subunit structure, amino-acid composition and metal content of the homogenous enzyme
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1981
Homo sapiens
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Comparative studies on AMP-deaminase-VII. Purification and some properties of the enzyme from crayfish Orconectes limosus tail muscle
Comp. Biochem. Physiol. B
72
127-132
1982
Faxonius limosus
-
brenda
Raffin, J.P.
AMP deaminase from the gill of the mullet Chelon labrosus R.: purification and effects of pH, phosphate and monovalent cations
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75
465-469
1983
Chelon labrosus
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Raffin, J.P.
AMP deaminase from dogfish erythrocytes: purification and some properties
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1983
Scyliorhinus canicula
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Kaletha, K.
Regulatory properties of 14-day embryo and adult hen skeletal muscle AMP-deaminase. The influence of pH on the enzyme activity
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Gallus gallus
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Purification and characterization of pig heart AMP-deaminase
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165B
501-504
1984
Sus scrofa
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Raffin, J.P.
Purification and properties of trout gill AMP deaminase
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154
55-63
1984
Oncorhynchus mykiss
-
brenda
Spychala, I.; Marszalek, J.; Kucharczyk, E.
AMP deaminases of rat small intestine
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1986
Rattus norvegicus
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Regulatory properties of AMP deaminase isoenzymes from rabbit red muscle
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242
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1987
Oryctolagus cuniculus
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Kaletha, K.; Nowak, G.
Developmental forms of human skeletal-muscle AMP deaminase. The kinetic and regulatory properties of the enzyme
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1988
Homo sapiens
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Ito, K.; Yamamoto, H.; Mizugaki, M.
Purification and general properties of AMP deaminase from sheep brain
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1988
Ovis aries
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Mahnke-Zizelman, D.K.; Tullson, P.C.; Sabina, R.L.
Novel aspects of tetramer assembly and N-terminal domain structure and function are revealed by recombinant expression of human AMP deaminase isoforms
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Homo sapiens
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Yeast AMP deaminase. Catalytic activity in Schizosaccharomyces pombe and chromosomal location in Saccharomyces cerevisiae
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1993
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Divergent N-terminal regions in AMP deaminase and isoform-specific catalytic properties of the enzymes
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321
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1995
Homo sapiens
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Ranieri-Raggi, M.; Ronca, F.; Sabbatini, A.; Raggi, A.
Regulation of skeletal-muscle AMP deaminase: involvement of histidine residues in the pH-dependent inhibition of the rabbit enzyme by ATP
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309
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1995
Oryctolagus cuniculus
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Thompson, A.; Hall, C.; Gunasekaran, M.
Properties of adenosine monophosphate deaminase of Candida albicans
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96
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1998
Candida albicans
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Spychala, J.; Marzalek, J.
Regulatory properties of AMP deaminases from rat tissues
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23
1155-1159
1991
Rattus norvegicus
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Nowak, G.; Kaletha, K.
Purification and properties of AMP-deaminase from human kidney
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47
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1992
Homo sapiens
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Lushchak, V.I.; Storey, K.B.
Effect of exercise on the properties of AMP-deaminase from trout white muscle
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26
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1994
Oncorhynchus mykiss
-
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Nagel-Starczynowska, G.; Kaletha, K.
AMP-deaminase from human uterine smooth muscle: the effect of DTNB treatment on kinetic and regulatory properties of the enzyme
Biochim. Biophys. Acta
1164
261-267
1993
Homo sapiens
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Kaletha, K.; Thebaul, M.; Raffin, J.P.
Comparative studies on heart and skeletal muscle AMP-deaminase from rainbow trout (Salmo gairdneri)
Comp. Biochem. Physiol. B
99
751-754
1991
Oncorhynchus mykiss
brenda
Raffin, J.P.; Izem, L.; Thebault, M.T.
Amplification of myoadenylate deaminase during evolution-II. Purification and properties of the enzyme from two elasmobranch fish, Scyliorhinus canicula and Raja clavata
Comp. Biochem. Physiol. B
106
999-1007
1993
Raja clavata, Scyliorhinus canicula
-
brenda
Lushchak, V.I.; Smirnova, Y.D.; Storey, K.B.
AMP-deaminase from sea scorpion white muscle: properties and redistribution under hypoxia
Comp. Biochem. Physiol. B
119
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1998
Sciaena umbra, Scorpaena porcus
-
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Hu, B.; Altschuld, R.A.; Hohl, C.M.
Adenosine stimulation of AMP deaminase activity in adult rat cardiac myocytes
Am. J. Physiol.
264
C48-53
1993
Rattus norvegicus
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Rundell, K.W.; Tullson, P.C.; Terjung, R.L.
Altered kinetics of AMP deaminase by myosin binding
Am. J. Physiol.
263
C294-299
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Rattus norvegicus
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Homo sapiens
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Homo sapiens
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Homo sapiens
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Comparative immunologic and kinetic evaluation of AMP-deaminase isolated from normal human liver and hepatocellular carcinoma (HCC)
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Homo sapiens
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Xu, J.; Zhang, H.Y.; Xie, C.H.; Xue, H.W.; Dijkhuis, P.; Liu, C.M.
EMBRYONIC FACTOR 1 encodes an AMP deaminase and is essential for the zygote to embryo transition in Arabidopsis
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Arabidopsis thaliana (O80452)
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Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. A new model for substrate interactions at a dinuclear cocatalytic Zn site
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Oryctolagus cuniculus
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Mangani, S.; Benvenuti, M.; Moir, A.J.; Ranieri-Raggi, M.; Martini, D.; Sabbatini, A.R.; Raggi, A.
Characterization of the metallocenter of rabbit skeletal muscle AMP deaminase. Evidence for a dinuclear zinc site
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Oryctolagus cuniculus
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Remote reperfusion lung injury is associated with AMP deaminase 3 activation and attenuated by inosine monophosphate
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Mus musculus
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Cyprinus carpio
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Sabina, R.L.; Waldenstroem, A.; Ronquist, G.
The contribution of Ca2+ calmodulin activation of human erythrocyte AMP deaminase (isoform E) to the erythrocyte metabolic dysregulation of familial phosphofructokinase deficiency
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Homo sapiens
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Homo sapiens
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Adenine nucleotide pool perturbation is a metabolic trigger for AMP deaminase inhibitor-based herbicide toxicity
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Arabidopsis thaliana
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Homo sapiens
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Dieni, C.A.; Storey, K.B.
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Lithobates sylvaticus
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Homo sapiens
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Molecular characterization and expression patterns of AMP deaminase1 (AMPD1) in porcine skeletal muscle
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Sus scrofa (B5SYT7), Sus scrofa
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Lushchak, V.I.; Husak, V.V.; Storey, J.M.; Storey, K.B.
AMP-deaminase from goldfish white muscle: regulatory properties and redistribution under exposure to high environmental oxygen level
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Carassius auratus
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Szydlowska, M.; Roszkowska, A.
Expression patterns of AMP-deaminase isozymes in human hepatocellular carcinoma (HCC)
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Homo sapiens
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Alessandrini, L.; Ciuffreda, P.; Pavlovic, R.; Santaniello, E.
Activity of adenosine deaminase and adenylate deaminase on adenosine and 2, 3-isopropylidene adenosine: role of the protecting group at different pH values
Nucleosides Nucleotides Nucleic Acids
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Aspergillus sp.
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Borkowski, T.; Orlewska, C.; Slominska, E.M.; Yuen, A.; Lipinski, M.; Rybakowska, I.; Foks, H.; Kaletha, K.K.; Yacoub, M.H.; Smolenski, R.T.
Pharmacological inhibition of AMP-deaminase in rat cardiac myocytes
Nucleosides Nucleotides Nucleic Acids
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Homo sapiens, Rattus norvegicus
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Borkowski, T.; Lipinski, M.; Kaminski, R.; Krzyminska-Stasiuk, E.; Langowska, M.; Raczak, G.; Slominska, E.M.; Smolenski, R.T.
Modulation of AMP deaminase in rat hearts subjected to ischemia and reperfusion by purine riboside
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Rattus norvegicus
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Lindell, S.; Maechling, S.; Sabina, R.
Synthesis and biochemical testing of 3-(carboxyphenylethyl)imidazo[2,1-f] [1,2,4]triazines as inhibitors of AMP deaminase
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Arabidopsis thaliana, Homo sapiens
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Taegtmeyer, A.B.; Breen, J.B.; Rogers, P.; Johnson, P.H.; Smith, J.; Smolenski, R.T.; Banner, N.R.; Yacoub, M.H.; Barton, P.J.
Effect of adenosine monophosphate deaminase-1 C34T allele on the requirement for donor inotropic support and on the incidence of early graft dysfunction after cardiac transplantation
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Homo sapiens
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Kaminsky, Y.; Kosenko, E.
AMP deaminase and adenosine deaminase activities in liver and brain regions in acute ammonia intoxication and subacute toxic hepatitis
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Rattus norvegicus
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Swieca, A.; Rybakowska, I.; Milczarek, R.; Klimek, J.; Kaletha, K.
AMP-deaminase from developing human placenta
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Homo sapiens
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Rybakowska, I.; Swieca, A.; Milczarek, R.; Klimek, J.; Kaletha, K.
AMP-deaminase from human preterm placenta - kinetic regulatory properties of enzyme
Placenta
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Homo sapiens
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Lee, S.; Wang, Y.; Kim, S.O.; Han, J.
AMPD3 is involved in anthrax LeTx-induced macrophage cell death
Protein Cell
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2011
Mus musculus
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Rybakowska, I.; Szydlowska, M.; Szrok, S.; Bakula, S.; Kaletha, K.
AMP-deaminase from thymus of patients with myasthenia gravis
Nucleosides Nucleotides Nucleic Acids
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Homo sapiens
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Li, S.; Qian, Y.; Liang, Y.; Chen, X.; Zhao, M.; Guo, Y.; Pang, Z.
Overproduction, purification and characterization of adenylate deaminase from Aspergillus oryzae
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Aspergillus oryzae, Aspergillus oryzae 3811
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Ronca, F.; Raggi, A.
Role of the HPRG component of striated muscle AMP deaminase in the stability and cellular behaviour of the enzyme
Biomolecules
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Rattus norvegicus (P10759), Oryctolagus cuniculus (P81072), Gallus gallus (P81073)
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Li, S.; Chen, L.; Hu, Y.; Fang, G.; Zhao, M.; Guo, Y.; Pang, Z.
Enzymatic production of 5-inosinic acid by AMP deaminase from a newly isolated Aspergillus oryzae
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Aspergillus oryzae, Aspergillus oryzae GX-AD08
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Okado, N.; Sugi, M.; Ueda, M.; Mizuhashi, F.; Lynch, B.S.; Vo, T.D.; Roberts, A.S.
Safety evaluation of AMP deaminase from Aspergillus oryzae
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Aspergillus oryzae, Aspergillus oryzae DEA262
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Rybakowska, I.M.; Bakula, S.; Kaletha, K.
Isozymes of AMP-deaminase in muscles Myasthenia Gravis patients
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Homo sapiens (P23109), Homo sapiens (Q01432), Homo sapiens (Q01433), Homo sapiens
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Zhang, X.K.; Nie, M.Y.; Chen, J.; Wei, L.J.; Hua, Q.
Multicopy integrants of crt genes and co-expression of AMP deaminase improve lycopene production in Yarrowia lipolytica
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Yarrowia lipolytica
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Kouzu, H.; Miki, T.; Tanno, M.; Kuno, A.; Yano, T.; Itoh, T.; Sato, T.; Sunaga, D.; Murase, H.; Tobisawa, T.; Ogasawara, M.; Ishikawa, S.; Miura, T.
Excessive degradation of adenine nucleotides by up-regulated AMP deaminase underlies afterload-induced diastolic dysfunction in the type 2 diabetic heart
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2015
Homo sapiens
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Joshi, P.R.; Apitz, T.; Zierz, S.
Normal activities of AMP-deaminase and adenylate kinase in patients with McArdle disease
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Homo sapiens
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Chew, B.; Fisk, I.; Fray, R.; Tucker, G.; Bodi, Z.; Ferguson, A.; Xia, W.; Seymour, G.
The effect of adenosine monophosphate deaminase overexpression on the accumulation of umami-related metabolites in tomatoes
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Solanum lycopersicum
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Lanaspa, M.A.; Epperson, L.E.; Li, N.; Cicerchi, C.; Garcia, G.E.; Roncal-Jimenez, C.A.; Trostel, J.; Jain, S.; Mant, C.T.; Rivard, C.J.; Ishimoto, T.; Shimada, M.; Sanchez-Lozada, L.G.; Nakagawa, T.; Jani, A.; Stenvinkel, P.; Martin, S.L.; Johnson, R.J.
Opposing activity changes in AMP deaminase and AMP-activated protein kinase in the hibernating ground squirrel
PLoS ONE
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2015
Ictidomys tridecemlineatus (A0A287DGA3)
brenda