Information on EC 3.5.4.6 - AMP deaminase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.5.4.6
-
RECOMMENDED NAME
GeneOntology No.
AMP deaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
AMP + H2O = IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O = IMP + NH3
show the reaction diagram
enzyme is associated to the histidine-proline-rich-glycoprotein HPRG via its catalytic subunit in a protein-protein complex
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amidine hydrolysis
-
-
-
-
Deamination
-
-
PATHWAY
KEGG Link
MetaCyc Link
adenosine nucleotides degradation I
-
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Purine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
AMP aminohydrolase
cf. EC 3.5.4.17 adenosine-phosphate deaminase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5'-adenosine monophosphate deaminase
-
-
5'-adenosine monophosphate deaminase
-
-
5'-adenosine monophosphate deaminase
B5SYT7
-
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
-
-
adenyl deaminase
-
-
-
-
adenylate aminohydrolase
-
-
-
-
adenylate deaminase
-
-
-
-
adenylate deaminase
-
-
adenylate deaminase
-
-
adenylate desaminase
-
-
-
-
adenylic acid deaminase
-
-
-
-
adenylic deaminase
-
-
-
-
AMP aminase
-
-
-
-
AMP deaminase
-
-
AMP deaminase
-
-
AMP deaminase
-
-
AMP deaminase 3
-
-
AMP deaminase H-type
-
-
-
-
AMP deaminase isoform E
-
-
AMP deaminase type 3
-
-
AMP deaminase1
B5SYT7
-
AMP-aminohydrolase
-
-
AMP-aminohydrolase
-
-
AMP-deaminase
-
-
AMP-deaminase
-
-
AMP-deaminase
-
-
AmpD
-
-
AMPD1
-
-
AMPD1
-
isozyme
AMPD1
B5SYT7
-
AMPD3
-
isozyme
AMPD3
-
-
AMPD3
-
isozyme
deaminase, adenylate
-
-
-
-
embryonic factor 1
-
encodes an AMP deaminase
embryonic factor 1
-
gene that encodes AMP deaminase
EMBRYONIC FACTOR1
-
-
Erythrocyte AMP deaminase
-
-
-
-
FAC1
-
gene that encodes AMP deaminase
Heart-type AMPD
-
-
-
-
Myoadenylate deaminase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9025-10-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Columbia
-
-
Manually annotated by BRENDA team
Mongrel dog
-
-
Manually annotated by BRENDA team
goldfish
-
-
Manually annotated by BRENDA team
3 genetic types: 1. fast-growing standard, a slow-growing French 'Label Rouge' type, and a heavy line type
-
-
Manually annotated by BRENDA team
4 isoenzymes
-
-
Manually annotated by BRENDA team
AMPD1, AMPD2 and AMPD3
-
-
Manually annotated by BRENDA team
C34T mutation of the AMPD1 gene is detected in a elite, male white endurance runner (28 years of age). World class status in endurance running can be reached despite partial deficiency in muscle AMPD
-
-
Manually annotated by BRENDA team
2 isozymes
-
-
Manually annotated by BRENDA team
skate
-
-
Manually annotated by BRENDA team
also known as Lithobates sylvaticus
-
-
Manually annotated by BRENDA team
AMPD1,2 and 3
-
-
Manually annotated by BRENDA team
form I and II
-
-
Manually annotated by BRENDA team
free and myosin-bound form
-
-
Manually annotated by BRENDA team
strain JM1901; yeast
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae JM1901
strain JM1901
-
-
Manually annotated by BRENDA team
Schizosaccharomyces pombe 972
strain 972
-
-
Manually annotated by BRENDA team
Sciaena umbra
corb
-
-
Manually annotated by BRENDA team
sea scorpion
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
AMP deaminase 3 is mutated in one of the mutant clones resistant to anthrax lethal toxin-induced death, AMPD3 deficiency does not affect anthrax lethal toxin entering cells and the cleavage of mitogen-activated protein kinase kinase by lethal factor inside cells, but does impair a downstream event that is linked to cell death. Restoration of anthrax lethal toxin sensitivity with ectopic reconstitution of AMPD3 expression
physiological function
-
during pregnancy the isoform composition of human placental AMP-deaminase changes as an adaptation of enzyme to changing metabolic requirements of the growing fetus, overview
physiological function
-
requirement of AMPD3 in anthrax lethal toxin-induced cell death of RAW 264.7 cells
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2',3'-isopropylidene adenosine + H2O
2',3'-O-(1-methylethylidene)inosine + NH3
show the reaction diagram
-
low activity
-
-
?
5'-AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
5-deoxyadenylic acid + H2O
dIMP + NH3
show the reaction diagram
-
at 7% or less the rate of AMP
-
-
?
5-deoxyadenylic acid + H2O
dIMP + NH3
show the reaction diagram
-
at 7% or less the rate of AMP
-
-
?
adenosine + H2O
inosine + NH3
show the reaction diagram
-
the activity of AMPDA with adenosine is not influenced by variation of pH values between 4 and 7, the highest activity is at pH 8
-
-
?
adenosine 5'-monosulfate + H2O
inosine 5'-monosulfate + NH3
show the reaction diagram
-
-
-
-
?
adenosine phosphoramidate + H2O
?
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
ir
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
ir
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
ir
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
ir
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
r
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
ir
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
Scorpaena porcus, Sciaena umbra
-
-
-
-
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
the enzyme converts AMP to IMP to maintain the energy potential
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
Schizosaccharomyces pombe 972, Saccharomyces cerevisiae JM1901
-
-
-
?
additional information
?
-
-
key enzyme of nucleotide breakdown is involved in regulation of adenine nucleotide pool in the liver
-
-
-
additional information
?
-
-
6 lysine residues are critical for the pH-dependent positive homotropic cooperativity behaviour of the enzyme, the lysines form a regulatory anionic site to which AMP must bind to stimulate the enzyme at alkaline pH
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
ir
AMP + H2O
IMP + NH3
show the reaction diagram
-
the enzyme converts AMP to IMP to maintain the energy potential
-
-
?
additional information
?
-
-
key enzyme of nucleotide breakdown is involved in regulation of adenine nucleotide pool in the liver
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activates
Ca2+
-
activates erythrocyte AMP deaminase [isoform E (AMPD3)] through a protein-protein interaction between calmodulin and the N-terminal domain of the AMPD3 polypeptide
Cs+
-
activates
K+
-
activates
K+
-
stabilizing the enzyme structure
K+
-
activates at low concentrations of 100-150 mM, in the presence of 100 mM K+ enzyme activity is increased by 1.7fold
K+
-
activates AMPD at low concentrations, with maximal activation (1.9fold) at about 80 mM
KCl
-
100-150 mM activates
KCl
-
stimulates, no stimulation of the trinitrobenzene sulfonic acid-desensitized enzyme due to blockage of the activation anionic site
Li+
-
activates
Mg2+
-
activates
Na+
-
activates
Na+
-
activates at low concentrations of 100-150 mM, in the presence of 100 mM Na+ enzyme activity is increased by 2.4fold
Na+
-
activates AMPD at low concentrations, with maximal activation (1.3fold) at about 80 mM
NaCl
-
100-150 mM activates
Rb+
-
activates
Zn2+
-
human muscle AMP-deaminase probably a zinc metalloenzyme
Zn2+
-
activates
Zn2+
-
enzyme HPRG component binds to Zn2+
Zn2+
-
dinuclear cocatalytic Zn site, the two Zn2+ ions in the AMPD metallocenter operate together as a single catalytic unit, but have independent functions
Zn2+
-
contains a dinuclear zinc site
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(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
-
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-(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'-IMP
-
in the absence of ATP
5,5-dithio-bis(2-nitrobenzoic acid)
-
reaction with thiol groups, leads to a decrease of 20-30% in Vmax
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+
-
at 10 mM Ca2+ inhibition of AMPD is 28%
Ca2+
-
25% inhibition at 10 mM
coformycin 5'-phosphate
-
-
coformycin 5'-phosphate
-
extremely potent AMPD inhibitor
Cu2+
-
0.005 mM, about 50% inhibition
deaminoformycin
-
0.0003 mM, strong inhibitor
deaminoformycin 5'-monophosphate
-
potent inhibitor
F-
-
above 2 mM
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
fluoride
-
8 mM fluoride reduce AMPD activity by 54%
fluoride
-
inhibits AMPD by about 66% at 8 mM
GTP
-
diethyl pyrocarbonate desensitizes inhibition
GTP
-
wild-type and trinitrobenzene sulfonic acid-desensitized enzyme
GTP
-
very strong inhibitor
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
iodoacetate
-
-
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
K+
-
inhibitory at concentrations higher than 80 mM
KCl
-
abover 150 mM
Mg2+
-
at 10 mM Mg2+ inhibition of AMPD is 13%
Mg2+
-
15% inhibition at 10 mM
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
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
Na+
-
inhibitory at concentrations higher than 80 mM
p-hydroxymercuribenzoate
-
-
phenylmethane-sulfonylfluoride
-
-
phosphate
-
weak
phosphate
-
-
phosphate
-
above 2 mM
phosphate
-
-
phosphate
-
competitive inhibitor, stabilizing the tetrameric enzyme structure
phosphate
-
above 0.5 mM
phosphate
-
10 mM phosphate lower activity by 39%
phosphate
-
inhibits AMPD by about 66% at 8 mM
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
Protamine sulfate
-
-
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
adenine
-
activates
adenosine
-
activates
adenosine
-
activates
ADP
-
activates
ADP
-
wild-type and trinitrobenzene sulfonic acid-desensitized enzyme
ADP
-
1 mM, activates
ADP
-
6.1fold activation at 2 mM
ADP
-
muscle AMPD is activated by Mg ADP-
ADP
-
strong activator, 1 mM ADP activates the enzyme by 3.2fold
ATP
-
activates
ATP
-
activates
ATP
-
1 mM, activates
ATP
-
3.7fold activation at 2 mM
ATP
-
muscle AMPD is activated by Mg ATP2-
ATP
-
strong activator, 1 mM ATP activates the enzyme by 1.7fold
Ca2+-calmodulin
-
-
-
Calmodulin
-
Ca2+-calmodulin activates erythrocyte AMPD in conditions of disturbed calcium homeostasis during sickle cell disease
citrate
-
activates
D-glucose
-
activates
dATP
-
activates
deoxyribose
-
activates
F-
-
slightly activates at concentrations up to 2 mM
glycerol
-
activates
hypoxanthine
-
activates
K+
Sciaena umbra, Scorpaena porcus
-
activates, 100-250 mM
Na+
Sciaena umbra, Scorpaena porcus
-
activates, 100 mM
native muscle proteinase
-
limited cleavage increases enzyme activity in presence of low concentrations of K+, probably due to removal of a fragment from the enzyme, which holds the enzyme in an inactive state, cleavage occurs e.g. during storage of both the muscle and the purified enzyme
-
phosphate
-
slightly activates at concentrations up to 2 mM
phosphate
-
0.5 mM, slight activation
purine riboside
-
10 min perfusion of the pre-ischemic heart or incubation of cardiomyocytes with 0.2 mM purine riboside results in activation of AMPD
Trypsin
-
limited cleavage increases enzyme activity in presence of low concentrations of K+, probably due to removal of a fragment from the enzyme, which holds the enzyme in an inactive state
-
K+
-
activates, 100-250 mM
additional information
-
the percentage of bound AMPD activity increases from 20 to 35% with the transition to the frozen state
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.4
-
AMP
-
crude enzyme extract, pH 6.5, 20C
0.6
0.8
AMP
-
AMPD1, endogenous, with 12.5 mM ATP
0.6
1
AMP
-
AMPD1, endogenous, without ATP
0.6
-
AMP
-
imidazole-eluted purified enzyme, pH 6.5, 20C
0.9
-
AMP
-
pH 6.5, 20C, wild-type enzyme
1
-
AMP
-
pH 6.5, 20C, trinitrobenzene sulfonic acid-treated enzyme
1
-
AMP
-
EDTA-eluted purified enzyme, pH 6.5, 20C
1.1
2.2
AMP
-
AMPD2, endogenous, with 12.5 mM ATP
1.4
-
AMP
-
recombinant AMPD1, with 12.5 mM ATP
1.71
-
AMP
-
free enzyme
2
-
AMP
-
-
2.2
-
AMP
-
myosin-bound enzyme
3.2
-
AMP
-
recombinant AMPD1, without ATP
3.5
-
AMP
-
recombinant AMPD2, with 12.5 mM ATP
4.5
9.9
AMP
-
AMPD2, endogenous, without ATP
11.5
-
AMP
-
recombinant AMPD2, without ATP
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics, stearyl-CoA influences the reaction kinetics
-
additional information
-
additional information
-
at pH 7.0 the reaction catalysed by AMP-deaminase from human preterm placenta follows a well depicted sigmoid-shaped kinetic profile, with a half-saturation constant (S0.5) value of about 9.2 mM. Phosphate hardly influences the kinetic profile diminishing the S0.5 constant value slightly to 8.1 mM. Addition into the medium of 1 mM adenine nucleotide, ADP or ATP, transforms the sigmoid-shaped profile of the control kinetic curve into a hyperbolic one, diminishing simultaneously the value of the S0.5 constant from 9.2 mM to 2.4 mM, respectively. Kinetic analysis, overview
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000601
-
deaminoformycin 5'-monophosphate
-
in 25 mM imidazole, pH 6.5, 150 mM potassium chloride, 2.4 mM AMP, and 0.2 mg/ml bovine serum albumin
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0003
-
1,3,4,6,7,8-hexahydro-4,6,6,7,8,8-hexamethyl-cyclopenta-gamma-2-benzopyran
-
IC50: 0.0003 mM
0.0003
-
1-(5,6,7,8-tetrahydro)3,5,5,6,8,8-hexamethyl-2-naphthalenyl-ethanone
-
IC50: 0.0003 mM
0.01
-
1-n-butyl-3-methylimidazolium chloride
-
IC50: 0.01 mM
0.01
-
1-n-butyl-3-methylimidazolium p-tosylate
-
IC50: 0.01 mM
0.005
-
1-n-butyl-3-methylimidazolium tetrafluoroborate
-
IC50: 0.005 mM
0.005
-
1-n-butyl-3-methylimidazolium tetrafluorophosphate
-
IC50: 0.005 mM
0.0003
-
1-t-butyl-3,5-dimethyl-2,4,6-trinitrobenzene
-
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
-
-
0.0009
-
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
pH and temperature not specified in the publication
0.0005
-
4-acetyl-1-t-butyl-3,5-dimethyl-2,6-dinitrobenzene
-
IC50: 0.0005 mM
0.08
-
GTP
-
free AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25C
0.1
-
GTP
-
myosin-bound AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25C
0.23
-
IMP
-
myosin-bound AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25C
162
-
K+
-
myosin-bound AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25C
702
-
K+
-
free AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25C
0.05
-
N-(2,3,4,6-tetra-O-acetyl-beta-D-glucopyranosyl)pyridinium bromide
-
IC50: 0.05 mM
0.5
-
N-(2,3,4,6-tetra-O-acetyl-beta-D-glucopyranosyl)trimethylammonium bromide
-
IC50: 0.5 mM
133
-
Na+
-
myosin-bound AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25C
824
-
Na+
-
free AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25C
254
-
NH3
-
free AMPD from frozen skeletal muscle, in 50 mM MOPS buffer (pH 7.2), at 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.008
-
-
-
0.01
-
-
enzyme from 40th week-old placenta, in 0.1 M succinate buffer, pH 6.5, at 5 mM substrate (AMP) concentration, at 30C
0.025
-
-
enzyme from 33rd week-old placenta, in 0.1 M succinate buffer, pH 6.5, at 5 mM substrate (AMP) concentration, at 30C
0.037
-
-
enzyme from 25th week-old placenta, in 0.1 M succinate buffer, pH 6.5, at 5 mM substrate (AMP) concentration, at 30C
0.077
-
-
non significant differences in enzyme activity are observed between homogenates from HCC tumor fragments and tumor surrounding fragments of the liver, where the specific activity is about 0.077 micromole/min/mg of protein
0.18
1.25
-
-
5.7
-
-
-
125
-
-
delta M90 AMPD3 mutant
865
-
-
wild-type AMPD3
976
-
-
-
1000
-
Sciaena umbra, Scorpaena porcus
-
-
1100
-
-
purified enzyme
1850
-
-
wild-type AMPD1
2743
-
-
-
3112
-
-
DELTA L96 AMPD1 mutant
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.6
6.8
-
Tris-acetic acid buffer
6
6.2
-
succinate buffer
6
-
-
enzyme from cirrhotic liver
6.3
-
-
-
6.4
-
-
pH optimum about 6, depending on purification procedure and buffer
6.5
-
-
-
6.6
-
-
-
6.6
-
-
enzyme from normal liver
7
-
-
-
7
-
-
assay at
7.1
-
-
-
8
-
-
using adenosine as substrate
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
treatment of the enzyme with trinitrobenzene sulfonic acid at pH 7.2 results in a progressive increase in activity at pH 7.1, no effect on activity at pH 6.5
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
-
at pH values of 5.5, 7.0 and 7.5, AMPD shows 56, 80 and 54% of its optimal activity, respectively
6
7.2
-
pH 6.0: about 55% of maximal activity, pH 7.2: about 55% of maximal activity, normal liver
additional information
-
-
AMP-deaminase from preterm placenta is less sensitive to pH changes compared to the enzyme from the term organ
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
similar level of expression of AMPD2, but greater expression of AMPD3 than in neurons
Manually annotated by BRENDA team
-
the study fails to confirm a survival benefit among heart failure patients carrying the AMPD1 T-allele (C34T)
Manually annotated by BRENDA team
-
activity of adenosine monophosphate deaminase is significantly higher in chicken of the fast-growing type than in the slow-growing French 'Label Rouge' type, and in heavy line typ
Manually annotated by BRENDA team
-
lower level of expression of both AMPD2 and AMPD3 than neurons, and a lower expression of AMPD3 than astrocytes
Manually annotated by BRENDA team
-
significantly increased FAC1 expression in the zygote, early embryo and endosperm. During somatic embryogenesis, a high level of FAC1 expression is observed in developing embryos including putative embryogenic cells. FAC1 represents one of the earliest expressed genes known in plants. It may act through AMP depletion to provide sufficient energy for the zygote to proceed through development
Manually annotated by BRENDA team
-
AMP-deaminase plays a role in formation of NH3 by endometrium stroma cells and its release into extracellular space during acetylcholine stimulation
Manually annotated by BRENDA team
-
significantly increased FAC1 expression in the zygote, early embryo and endosperm
Manually annotated by BRENDA team
-
cardiac myocytes
Manually annotated by BRENDA team
-
potential major role for increased AMP deaminase activity in diastolic dysfunction
Manually annotated by BRENDA team
-
cortex and medulla
Manually annotated by BRENDA team
-
normal and cirrhotic
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
Sciaena umbra
-
-
Manually annotated by BRENDA team
-
white muscle
Manually annotated by BRENDA team
-
white muscle
Manually annotated by BRENDA team
-
from forebrain. In neurons AMPD2 exhibits 8fold greater expression than AMPD3
Manually annotated by BRENDA team
-
isozymes AMPD2 and AMPD3, but not isozyme AMPD1 are expressed in term placenta, the expression level of AMPD3 is a half of that presented by AMPD2
Manually annotated by BRENDA team
-
preterm placenta. During pregnancy the isoform composition of human placental AMP-deaminase changes. High catalytic efficiency of the enzyme at early phase of the pregnancy
Manually annotated by BRENDA team
-
a macrophage-like cell line sensitive to anthrax lethal toxin, i.e. LeTx, induced death
Manually annotated by BRENDA team
-
from back and hind leg
Manually annotated by BRENDA team
-
higher activity in white muscle compared to red muscle
Manually annotated by BRENDA team
B5SYT7
AMPD1 is expressed specifically in skeletal muscle
Manually annotated by BRENDA team
-
white skeletal muscle
Manually annotated by BRENDA team
-
smooth muscle
Manually annotated by BRENDA team
-
significantly increased FAC1 expression in the zygote, early embryo and endosperm
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
reversible association between the catalytic domain of the enzyme and the intracellular membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55000
-
-
subunit, SDS-PAGE
55000
-
-
the SDS-PAGE shows that the enzyme is not electrophoretically homogenous, with two bands present at a molecular mass between about 55000 and 60000 Da
60000
-
-
the SDS-PAGE shows that the enzyme is not electrophoretically homogenous, with two bands present at a molecular mass between about 55000 and 60000 Da
68000
-
-
SDS-PAGE, 92000 and 68000 Da fragments of the enzyme react with specific polyclonal anti-(human) AMPD2 antibodies
68000
-
-
SDS-PAGE
85000
-
-
SDS-PAGE
92000
-
-
SDS-PAGE, 92 and 68 kDa fragments of the enzyme react with specificpolyclonal anti-(human) AMPD2 antibodies
140000
400000
-
3 different oligomeric enzyme forms of 140 kDa, 280 kDa, and 400 kDa, gel filtration
145000
-
-
gel filtration
150000
-
-
gel filtration
160000
-
-
myosin-bound enzyme, SDS-PAGE
276000
-
-
sucrose density gradient centrifugation
285000
-
-
sucrose density gradient centrifugation
320000
-
-
calculation from sedimentation constant and diffusion coefficient
330000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 70000-95000, histidine-proline-rich-glycoprotein HPRG component, partially proteolyzed or deglycosylated, SDS-PAGE
?
-
x * 37000, SDS-PAGE
oligomer
-
x * 68000, at least 3 different oligomeric forms of the enzyme, probably dimers, tetramers, and hexamers, SDS-PAGE
tetramer
-
4 * 69000, SDS-PAGE
tetramer
-
4 * 83000, SDS-PAGE
tetramer
-
4 * 80000-85000
tetramer
-
4*37000, SDS-PAGE
tetramer
-
4 * 80000, stabilized by phosphate
tetramer
-
2 * 85000 (catalytic subunits) + 2 * 70000 (histidine-proline-rich-glycoprotein subunits)
additional information
-
enzyme contains a histidine-proline-rich-glycoprotein HPRG component, bound via its catalytic subunit in a protein-protein complex, which is critical for the enzyme stability, disulfide bridges are involved in formation of enzyme conformation
additional information
-
in contrast to AMP-deaminase isolated from the normal, healthy liver, where presence of relatively large (68 kDa) protein fragment is also detected, only smaller protein fragments are identified, while SDS-PAGE of AMP-deaminase isolated from the cirrhotic liver is performed
additional information
-
in enzyme from healthy liver beside immunologically reactive 92000 Da protein fragment, corresponding to the full size of the enzyme subunit, also a smaller, immunologically reactive protein fragment 68000 Da is identified in the gel. When SDS-PAGE of AMP-deaminase isolated from neo-plasmatic liver is performed only presence of protein fragment 68000 Da was detected
additional information
-
presence of two species of 173 kDa and 309 kDa being consistent with the existence of a dimer-tetramer equilibrium
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
enzyme contains a histidine-proline-rich-glycoprotein HPRG component
phosphoprotein
-
the reversible phosphorylation adjusts enzyme function for an optimal role in controlling cellular adenylate levels in ischemic frozen muscle
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3.3 A globular catalytic domain X-ray crystal structure with a bound herbicide-based transition state inhibitor (coformycin 5'-phosphate)
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
-
slowly reduces its activity on the both sides of the optimum pH 6.3, at pH values of 5.5, 7.0 and 7.5, AMPD shows 13, 31 and 65% lower activity, respectively
6.8
-
-
highest stability
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
4
-
at high concentrations, 10 days
50
-
-
heating at 50C quickly destroys AMPD activity when the enzyme is incubated in distilled water, AMPD remains fully active over 30 min in the presence 1 M KCl at 50C
additional information
-
-
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
heating in the presence of low KCl (150 mM) results in a rapid loss in activity with only 25% of initial activity being left after 30 min, about half of the initial activity remains after heating for 30 min in 25 mM histidine solution, solution, incubation in imidazole or phosphate solutions results in greater stability over 30 min of heating with AMPD activity decreasing by about 20%
-
freezing, unstable
-
sulfhydryl reagents and monovalent cations in high concentrations stabilize
-
an apparent 10000 Da reduction in molecular mass of the native 85000 Da enzyme subunit with its conversion to a 75000 Da core is observed on storage of AMPD
-
EDTA stabilizes the purified enzyme during storage
-
phosphate stabilizes the tetrameric structure of the enzyme
-
repeated freezing and thawing, stable
-
ATP, ADP, GTP and alkali metal ions protect against heat inactivation
-
enzyme is associated to the histidine-proline-rich-glycoprotein HPRG via its catalytic subunit in a protein-protein complex, which is critical for the enzyme stability
-
additional information
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-4C, following the purification process when stored in 1 M KCl, 1 month, the enzyme is highly stable showing virtually no change in activity
-
2-4C, 1 M KCl, at least 1 month, no loss of activity
-
0-4C or -20C for up to 10 days, 30 mg/ml protein
-
-20C, 4 months, less than 10% loss of activity
-
4C, purified enzyme, loss of 50% activity within 1 week in absence of EDTA, in presence of EDTA it is stable for 10 days, fragmentation occurs at 4C
-
storage of the muscle material as well as the purified enzyme increases the enzyme activity due to limited proteolytic cleavage
-
4C, several days, small loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
phosphocellulose column chromatography
-
phosphocellulose column chromatography
-
expression in Escherichia coli
-
expression of AMPD1 and AMPD3 in Sf9 cells
-
native enzyme from human term and preterm placenta
-
partially
-
phosphocellulose column chromatography
-
both native enzyme and its histidine-proline-rich-glycoprotein HPRG component, the latter being completely separated from the enzyme and its catalytic subunit by Zn2+-affinity chromatography including presence of 1 M KCl
-
Sephadex G50 gel filtration
-
-
Sciaena umbra, Scorpaena porcus
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Sf9 cells
-
expression in Escherichia coli
-
expression of AMPD1 and AMPD3 in Sf9 cells
-
AMPD3 expressed in Sf9 cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
during pregnancy the activity of AMP-deaminase in developing human placenta gradually decreases, being in homogenates of mature, term placenta (about 40 weeks of gestation) one fourth to one third of that in homogenates of immature (about 25 weeks of gestation) organ
-
AMP deaminase in the liver is elevated by 4.2fold in models of hepatotoxic injury as compared with controls. In acute hyperammonemia, activity of AMP deaminase increases by 59% in the neocortex. In the hippocampus of hyperammonemic rats, AMP deaminase activity is increased by 48%. Subacute hepatitis leads to 228% increase in AMP deaminase activity
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C34T
-
mutation of the AMPD1 gene is detected in a elite, male white endurance runner (28 years of age). World class status in endurance running can be reached despite partial deficiency in muscle AMPD
C34T
-
devoid of AMPD activity
DELTAL96
-
AMPD1 mutant, higher specific activity
DELTAM90
-
AMPD3 mutant, lower specific activity
additional information
-
AMP deaminase 3 is mutated in one of the mutant clones resistant to anthrax lethal toxin-induced death, restoration of anthrax lethal toxin sensitivity with ectopic reconstitution of AMPD3 expression
additional information
B5SYT7
a single nucleotide polymorphism (T426C) in exon 12 of the AMPD1 gene is significantly associated with loin muscle area trait, loin muscle height, and average backfat thickness
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
the C34T T allele of the adenosine monophosphate deaminase-1 gene is associated with improved outcome in patients with cardiac dysfunction. Possession of the adenosine monophosphate deaminase-1 T allele is associated with decreased inotropic requirements before heart donation
medicine
-
AMPD3 is a potential candidate for a pharmacological therapeutic strategy for remote reperfusion lung injury
analysis
-
assessment of synthetic nitro- and polycyclic musks, imidazolium ionic liquids and N-glucopyranosyl ammonium salts