Information on EC 3.5.4.17 - adenosine-phosphate deaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.5.4.17
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RECOMMENDED NAME
GeneOntology No.
adenosine-phosphate deaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ADP + H2O = IDP + NH3
show the reaction diagram
(2)
-
-
-
AMP + H2O = IMP + NH3
show the reaction diagram
(1)
-
-
-
ATP + H2O = ITP + NH3
show the reaction diagram
(3)
-
-
-
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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SYSTEMATIC NAME
IUBMB Comments
adenosine-phosphate aminohydrolase
Acts on AMP, ADP, ATP, NAD+ and adenosine, in decreasing order of activity. The bacterial enzyme can also accept the deoxy derivatives. cf. EC 3.5.4.6, AMP deaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-20-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
var. azotovorans strain Berre S
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-
Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2',3'-cAMP + H2O
2',3'-cIMP + NH3
show the reaction diagram
2'-deoxyadenosine + H2O
2'-deoxyinosine + NH3
show the reaction diagram
3'-AMP + H2O
3'-IMP + NH3
show the reaction diagram
3'-deoxyadenosine + H2O
3'-deoxyinosine + NH3
show the reaction diagram
5'-AMP + H2O
5'-IMP + NH3
show the reaction diagram
5'-deoxyadenosine + H2O
5'-deoxyinosine + NH3
show the reaction diagram
adenosine + H2O
inosine + NH3
show the reaction diagram
adenosine 3'-phenyl phosphonate + H2O
inosine 3'-phenylphosphonate + NH3
show the reaction diagram
ADP + H2O
IDP + NH3
show the reaction diagram
ADP-ribose + H2O
IDP-ribose + NH3
show the reaction diagram
-
-
-
-
ir
AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
ir
ApA + H2O
IpI + NH3
show the reaction diagram
-
37.6% of the activity with 2',3'-cAMP
-
-
?
ApC + H2O
IpC + NH3
show the reaction diagram
-
41.8% of the activity with 2',3'-cAMP
-
-
?
ApCpC + H2O
IpCpC + NH3
show the reaction diagram
-
12.1% of the activity with 2',3'-cAMP
-
-
?
ApG + H2O
IpG + NH3
show the reaction diagram
-
30.9% of the activity with 2',3'-cAMP
-
-
?
ApU + H2O
IpU + NH3
show the reaction diagram
-
51.5% of the activity with 2',3'-cAMP
-
-
?
ATP + H2O
ITP + NH3
show the reaction diagram
dADP + H2O
dIDP + NH3
show the reaction diagram
-
-
-
-
ir
dAMP + H2O
dIMP + NH3
show the reaction diagram
-
-
-
-
ir
dATP + H2O
dITP + NH3
show the reaction diagram
-
-
-
-
ir
deoxyadenosine + H2O
deoxyinosine + NH3
show the reaction diagram
-
-
-
-
ir
NAD+ + H2O
nicotinamide-hypoxanthine dinucleotide + NH3
show the reaction diagram
additional information
?
-
-
the enzyme deaminates 5'-hydroxyl terminal adenosine residues in dinucleotides and trinucleotides, but not the 3'-hydroxyl terminal one in dinucleotides. The 5'-hydroxyl group of the ribose moiety is necessary for the substrate binding and catalytic activity of the squid enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
50% of the activation with Ca2+
Ca2+
-
enhances activity
Mg2+
-
50% of the activation with Ca2+
Mn2+
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activates at acidic pH. At neutral and alkaline pH it acts as inhibitor
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-AMP
-
inhibits deamination of ATP
3'-AMP
-
inhibits deamination of ATP
3'-IMP
-
competitive inhibition of deamination of adenosine 3'-phenylphosphonate
adenine
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competitive inhibition of deamination of adenosine 3'-phenylphosphonate
adenosine
-
inhibits deamination of ATP
Ag+
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0.5 mM, complete inhibition of deamination of ATP
beta,beta-dimethyl glutarate
-
-
CN-
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non-competitive inhibition at low concentrations
Hg2+
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0.5 mM, complete inhibition of deamination of ATP
Inosine
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competitive inhibition of deamination of adenosine 3'-phenylphosphonate
p-mercuribenzoate
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purine riboside
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competitive inhibition of deamination of adenosine 3'-phenylphosphonate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cl-
-
activates the deamination of ATP, NAD+, ADP and 5'-AMP to the extent of 40%, 30%, 30% and 14%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 0.13
2',3'-cAMP
0.065
2',3'-Cyclic AMP
-
-
0.071 - 0.27
2'-deoxyadenosine
0.085 - 0.34
3'-AMP
0.067
3'-deoxyadenosine
-
-
0.047
5'-AMP
-
-
0.65
5'-deoxyadenosine
-
-
0.075 - 0.56
adenosine
0.067 - 0.14
adenosine 3'-phenylphosphonate
0.047
ADP
-
-
0.066
ATP
-
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0.072
NAD+
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 4
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deamination of adenosine 3'-phenylphosphonate
4 - 4.5
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deamination of 3'-AMP
4
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deamination of 2',3'-cAMP and 3'-AMP
4 - 4.5
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deamination of 3'-AMP
4.5 - 6.5
5.4 - 5.8
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deamination of NAD+
5.5
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immobilized enzyme
5.5 - 6.5
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deamination of ATP
5.5
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deamination of adenosine and 2'-deoxyadenosine
5.9 - 6.5
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deamination of ADP
6.5 - 7.5
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deamination of adenosine
6.8
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deamination of 5'-AMP
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 7
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pH 2.5: about 55% of maximal activity at pH 2.5 and at pH 7.0
3.5 - 6.5
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pH 3.5: about 65% of maximal activity, pH 6.5: about 40% of maximal activity, deamination of adenosine 3'-phenylphosphonate. pH 3.5: about 55% of maximal activity, pH 6.5: about 25% of maximal activity, deamination of 2',3'-cyclic AMP
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
free and immobilized enzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
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2 * 60000, SDS-PAGE
64000
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2 * 64000, SDS-PAGE
140000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 5.5
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45°C, 30 min, immobilized enzyme is stable
246707
5 - 6
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45°C, 30 min, free enzyme is stable
246707
6 - 7
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below 37°C, 20 mM phosphate buffer, stable
246710
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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stable for 3 days at room temperature
65
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pH 6.4, 6 min, 50% loss of activity. At pH 5.1 and 7.1, more than 90% loss of activity after 5 min
70
-
6 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme immobilized in polyacrylamide beads, the column is used several times over a 3 months period, no loss of activity
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stable to several cycles of freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, even a very dilute preparation does not lose any activity after storage for 1 month
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-20°C, indefinitely stable
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4°C, stable for 2 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE