Information on EC 3.5.4.6 - AMP deaminase and Organism(s) Homo sapiens

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Homo sapiens


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.4.6
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RECOMMENDED NAME
GeneOntology No.
AMP deaminase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
adenosine nucleotides degradation I
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purine metabolism
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Purine metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
AMP aminohydrolase
cf. EC 3.5.4.17 adenosine-phosphate deaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-10-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
additional information
?
-
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key enzyme of nucleotide breakdown is involved in regulation of adenine nucleotide pool in the liver
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-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
AMP + H2O
IMP + NH3
show the reaction diagram
additional information
?
-
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key enzyme of nucleotide breakdown is involved in regulation of adenine nucleotide pool in the liver
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-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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activates erythrocyte AMP deaminase [isoform E (AMPD3)] through a protein-protein interaction between calmodulin and the N-terminal domain of the AMPD3 polypeptide
Cs+
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activates
K+
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activates
Li+
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activates
Na+
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activates
Rb+
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activates
Zn2+
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human muscle AMP-deaminase probably a zinc metalloenzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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2'-AMP
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in the absence of ATP
2,3-diphosphoglyceric acid
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ATP counteracts inhibition
3'-AMP
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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
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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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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-(imidazo[2,1-f][1,2,4]triazin-7-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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5'-IMP
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in the absence of ATP
coformycin 5'-phosphate
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extremely potent AMPD inhibitor
phosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
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activates
Ca2+-calmodulin
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-
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Calmodulin
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Ca2+-calmodulin activates erythrocyte AMPD in conditions of disturbed calcium homeostasis during sickle cell disease
dATP
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activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 11.5
AMP
additional information
additional information
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 0.0057
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
0.1 - 0.37
3-[2-(imidazo[2,1-f][1,2,4]triazin-7-yl)ethyl]benzoic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.008
-
-
0.01
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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
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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
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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
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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
125
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delta M90 AMPD3 mutant
865
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wild-type AMPD3
1850
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wild-type AMPD1
3112
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DELTA L96 AMPD1 mutant
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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enzyme from cirrhotic liver
7
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assay at
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.2
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pH 6.0: about 55% of maximal activity, pH 7.2: about 55% of maximal activity, normal liver
additional information
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AMP-deaminase from preterm placenta is less sensitive to pH changes compared to the enzyme from the term organ
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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the study fails to confirm a survival benefit among heart failure patients carrying the AMPD1 T-allele (C34T)
Manually annotated by BRENDA team
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cortex and medulla
Manually annotated by BRENDA team
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skeletal muscle
Manually annotated by BRENDA team
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smooth muscle
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85000
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SDS-PAGE
92000
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SDS-PAGE, 92 and 68 kDa fragments of the enzyme react with specificpolyclonal anti-(human) AMPD2 antibodies
140000 - 400000
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3 different oligomeric enzyme forms of 140 kDa, 280 kDa, and 400 kDa, gel filtration
145000
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gel filtration
150000
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gel filtration
285000
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sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
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x * 68000, at least 3 different oligomeric forms of the enzyme, probably dimers, tetramers, and hexamers, SDS-PAGE
tetramer
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing, unstable
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sulfhydryl reagents and monovalent cations in high concentrations stabilize
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 4 months, less than 10% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression of AMPD1 and AMPD3 in Sf9 cells
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native enzyme from human term and preterm placenta
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partially
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phosphocellulose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression of AMPD1 and AMPD3 in Sf9 cells
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EXPRESSION
ORGANISM
UNIPROT
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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTAL96
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AMPD1 mutant, higher specific activity
DELTAM90
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AMPD3 mutant, lower specific activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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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