BRENDA - Enzyme Database

Catabolism of Ap3A and Ap4A in human plasma. Purification and characterization of a glycoprotein complex with 5'-nucleotide phosphodiesterase activity

Luthje, J.; Ogilvie, A.; Eur. J. Biochem. 149, 119-127 (1985)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.4.1
5'-nucleotides
-
Homo sapiens
3.1.4.1
ADP
-
Homo sapiens
3.1.4.1
AMP
-
Homo sapiens
3.1.4.1
CMP
-
Homo sapiens
3.1.4.1
CoA
-
Homo sapiens
3.1.4.1
EDTA
completely, inactivation reversed by Ca2+, Co2+ and, at best, with Zn2+
Homo sapiens
3.1.4.1
GTP
-
Homo sapiens
3.1.4.1
Mn2+
-
Homo sapiens
3.1.4.1
NAD+
-
Homo sapiens
3.1.4.1
NADH
-
Homo sapiens
3.1.4.1
NADP+
-
Homo sapiens
3.1.4.1
NADPH
-
Homo sapiens
3.1.4.1
terminal 3'-monophosphoryl group of substrates
-
Homo sapiens
3.1.4.1
UMP
-
Homo sapiens
3.6.1.29
EDTA
-
Homo sapiens
3.6.1.29
Mn2+
-
Homo sapiens
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.1.4.1
0.0006
-
diadenosine 5',5'''-P1,P4-tetraphosphate
Ap4A
Homo sapiens
3.1.4.1
0.001
-
diadenosine 5',5'''-P1,P3-triphosphate
Ap3A
Homo sapiens
3.6.1.29
0.0006
-
Ap4A
-
Homo sapiens
3.6.1.29
0.001
-
P1-P3-bis(5'-adenosyl) triphosphate
-
Homo sapiens
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.4.1
Ca2+
activation
Homo sapiens
3.1.4.1
Co2+
activation
Homo sapiens
3.1.4.1
divalent cations
activation
Homo sapiens
3.1.4.1
Mg2+
activation
Homo sapiens
3.1.4.1
Ni2+
slight activation
Homo sapiens
3.1.4.1
Zn2+
activation; physiologically bound
Homo sapiens
3.6.1.29
Ca2+
-
Homo sapiens
3.6.1.29
Mg2+
-
Homo sapiens
3.6.1.29
Zn2+
-
Homo sapiens
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.4.1
16000
-
x * 66000 + x * 45000 + x * 16000, enzyme has a complex structure, which is composed of subunits of different size, stoichiometry of the complex is still uncertain, SDS-PAGE
Homo sapiens
3.1.4.1
45000
-
x * 66000 + x * 45000 + x * 16000, enzyme has a complex structure, which is composed of subunits of different size, stoichiometry of the complex is still uncertain, SDS-PAGE
Homo sapiens
3.1.4.1
66000
-
x * 66000 + x * 45000 + x * 16000, enzyme has a complex structure, which is composed of subunits of different size, stoichiometry of the complex is still uncertain, SDS-PAGE
Homo sapiens
3.1.4.1
230000
-
gel filtration
Homo sapiens
3.6.1.29
230000
-
gel filtration
Homo sapiens
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3.1.4.1
diadenosine polyphosphate + H2O
Homo sapiens
phosphodiesterase can be considered as a catabolic enzyme
AMP
-
-
-
3.1.4.1
additional information
Homo sapiens
enzyme might function as a modulating factor of platelet aggregation
?
-
-
-
3.6.1.29
P1-P3-bis(5'-adenosyl) triphosphate + H2O
Homo sapiens
-
ADP + AMP
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.4.1
Homo sapiens
-
-
-
3.6.1.29
Homo sapiens
-
-
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
3.1.4.1
glycoprotein
-
Homo sapiens
3.6.1.29
glycoprotein
mannoside
Homo sapiens
Purification (Commentary)
EC Number
Commentary
Organism
3.1.4.1
-
Homo sapiens
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.4.1
blood plasma
-
Homo sapiens
-
3.6.1.29
plasma
-
Homo sapiens
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
3.1.4.1
additional information
-
-
Homo sapiens
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.4.1
adenosine 5'-P1-tetraphospho-P4-5'''-adenosine + H2O
-
208383
Homo sapiens
AMP + ATP
-
208383
Homo sapiens
?
3.1.4.1
ATP + H2O
-
208383
Homo sapiens
5'-AMP + diphosphate
-
-
-
?
3.1.4.1
diadenosine 5',5'''-P1,P3-triphosphate + H2O
-
208383
Homo sapiens
AMP + ADP
-
208383
Homo sapiens
?
3.1.4.1
diadenosine polyphosphate + H2O
phosphodiesterase can be considered as a catabolic enzyme
208383
Homo sapiens
AMP
-
-
-
-
3.1.4.1
dinucleotides + H2O
-
208383
Homo sapiens
?
-
-
-
?
3.1.4.1
additional information
no activity with p-nitrophenylthymidine 3'-phosphate
208383
Homo sapiens
?
-
-
-
-
3.1.4.1
additional information
broad substrate specificity
208383
Homo sapiens
?
-
-
-
-
3.1.4.1
additional information
enzyme might function as a modulating factor of platelet aggregation
208383
Homo sapiens
?
-
-
-
-
3.1.4.1
NAD+ + H2O
-
208383
Homo sapiens
5'-AMP + NMN
-
-
-
?
3.1.4.1
p-nitrophenylthymidine 5'-phosphate + H2O
-
208383
Homo sapiens
5'-TMP + p-nitrophenol
-
-
-
?
3.1.4.1
UTP + H2O
-
208383
Homo sapiens
UMP + diphosphate
-
208383
Homo sapiens
?
3.6.1.29
ATP + 2 H2O
-
208383
Homo sapiens
AMP + 2 phosphate
-
-
-
?
3.6.1.29
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
-
208383
Homo sapiens
AMP + ATP
-
-
-
?
3.6.1.29
NAD+ + H2O
-
208383
Homo sapiens
?
-
-
-
?
3.6.1.29
P1-P3-bis(5'-adenosyl) triphosphate + H2O
-
208383
Homo sapiens
ADP + AMP
-
-
-
?
3.6.1.29
thymidine 5'-monophosphate p-nitrophenylester + H2O
-
208383
Homo sapiens
?
-
-
-
?
3.6.1.29
UTP + H2O
-
208383
Homo sapiens
UMP + phosphate
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
3.1.4.1
?
x * 66000 + x * 45000 + x * 16000, enzyme has a complex structure, which is composed of subunits of different size, stoichiometry of the complex is still uncertain, SDS-PAGE
Homo sapiens
3.6.1.29
polymer
-
Homo sapiens
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.1.4.1
8
9
-
Homo sapiens
3.6.1.29
8.5
-
-
Homo sapiens
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.4.1
5'-nucleotides
-
Homo sapiens
3.1.4.1
ADP
-
Homo sapiens
3.1.4.1
AMP
-
Homo sapiens
3.1.4.1
CMP
-
Homo sapiens
3.1.4.1
CoA
-
Homo sapiens
3.1.4.1
EDTA
completely, inactivation reversed by Ca2+, Co2+ and, at best, with Zn2+
Homo sapiens
3.1.4.1
GTP
-
Homo sapiens
3.1.4.1
Mn2+
-
Homo sapiens
3.1.4.1
NAD+
-
Homo sapiens
3.1.4.1
NADH
-
Homo sapiens
3.1.4.1
NADP+
-
Homo sapiens
3.1.4.1
NADPH
-
Homo sapiens
3.1.4.1
terminal 3'-monophosphoryl group of substrates
-
Homo sapiens
3.1.4.1
UMP
-
Homo sapiens
3.6.1.29
EDTA
-
Homo sapiens
3.6.1.29
Mn2+
-
Homo sapiens
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.1.4.1
0.0006
-
diadenosine 5',5'''-P1,P4-tetraphosphate
Ap4A
Homo sapiens
3.1.4.1
0.001
-
diadenosine 5',5'''-P1,P3-triphosphate
Ap3A
Homo sapiens
3.6.1.29
0.0006
-
Ap4A
-
Homo sapiens
3.6.1.29
0.001
-
P1-P3-bis(5'-adenosyl) triphosphate
-
Homo sapiens
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
3.1.4.1
Ca2+
activation
Homo sapiens
3.1.4.1
Co2+
activation
Homo sapiens
3.1.4.1
divalent cations
activation
Homo sapiens
3.1.4.1
Mg2+
activation
Homo sapiens
3.1.4.1
Ni2+
slight activation
Homo sapiens
3.1.4.1
Zn2+
activation; physiologically bound
Homo sapiens
3.6.1.29
Ca2+
-
Homo sapiens
3.6.1.29
Mg2+
-
Homo sapiens
3.6.1.29
Zn2+
-
Homo sapiens
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.4.1
16000
-
x * 66000 + x * 45000 + x * 16000, enzyme has a complex structure, which is composed of subunits of different size, stoichiometry of the complex is still uncertain, SDS-PAGE
Homo sapiens
3.1.4.1
45000
-
x * 66000 + x * 45000 + x * 16000, enzyme has a complex structure, which is composed of subunits of different size, stoichiometry of the complex is still uncertain, SDS-PAGE
Homo sapiens
3.1.4.1
66000
-
x * 66000 + x * 45000 + x * 16000, enzyme has a complex structure, which is composed of subunits of different size, stoichiometry of the complex is still uncertain, SDS-PAGE
Homo sapiens
3.1.4.1
230000
-
gel filtration
Homo sapiens
3.6.1.29
230000
-
gel filtration
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3.1.4.1
diadenosine polyphosphate + H2O
Homo sapiens
phosphodiesterase can be considered as a catabolic enzyme
AMP
-
-
-
3.1.4.1
additional information
Homo sapiens
enzyme might function as a modulating factor of platelet aggregation
?
-
-
-
3.6.1.29
P1-P3-bis(5'-adenosyl) triphosphate + H2O
Homo sapiens
-
ADP + AMP
-
-
?
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
3.1.4.1
glycoprotein
-
Homo sapiens
3.6.1.29
glycoprotein
mannoside
Homo sapiens
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.4.1
-
Homo sapiens
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.4.1
blood plasma
-
Homo sapiens
-
3.6.1.29
plasma
-
Homo sapiens
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
3.1.4.1
additional information
-
-
Homo sapiens
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.4.1
adenosine 5'-P1-tetraphospho-P4-5'''-adenosine + H2O
-
208383
Homo sapiens
AMP + ATP
-
208383
Homo sapiens
?
3.1.4.1
ATP + H2O
-
208383
Homo sapiens
5'-AMP + diphosphate
-
-
-
?
3.1.4.1
diadenosine 5',5'''-P1,P3-triphosphate + H2O
-
208383
Homo sapiens
AMP + ADP
-
208383
Homo sapiens
?
3.1.4.1
diadenosine polyphosphate + H2O
phosphodiesterase can be considered as a catabolic enzyme
208383
Homo sapiens
AMP
-
-
-
-
3.1.4.1
dinucleotides + H2O
-
208383
Homo sapiens
?
-
-
-
?
3.1.4.1
additional information
no activity with p-nitrophenylthymidine 3'-phosphate
208383
Homo sapiens
?
-
-
-
-
3.1.4.1
additional information
broad substrate specificity
208383
Homo sapiens
?
-
-
-
-
3.1.4.1
additional information
enzyme might function as a modulating factor of platelet aggregation
208383
Homo sapiens
?
-
-
-
-
3.1.4.1
NAD+ + H2O
-
208383
Homo sapiens
5'-AMP + NMN
-
-
-
?
3.1.4.1
p-nitrophenylthymidine 5'-phosphate + H2O
-
208383
Homo sapiens
5'-TMP + p-nitrophenol
-
-
-
?
3.1.4.1
UTP + H2O
-
208383
Homo sapiens
UMP + diphosphate
-
208383
Homo sapiens
?
3.6.1.29
ATP + 2 H2O
-
208383
Homo sapiens
AMP + 2 phosphate
-
-
-
?
3.6.1.29
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
-
208383
Homo sapiens
AMP + ATP
-
-
-
?
3.6.1.29
NAD+ + H2O
-
208383
Homo sapiens
?
-
-
-
?
3.6.1.29
P1-P3-bis(5'-adenosyl) triphosphate + H2O
-
208383
Homo sapiens
ADP + AMP
-
-
-
?
3.6.1.29
thymidine 5'-monophosphate p-nitrophenylester + H2O
-
208383
Homo sapiens
?
-
-
-
?
3.6.1.29
UTP + H2O
-
208383
Homo sapiens
UMP + phosphate
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
3.1.4.1
?
x * 66000 + x * 45000 + x * 16000, enzyme has a complex structure, which is composed of subunits of different size, stoichiometry of the complex is still uncertain, SDS-PAGE
Homo sapiens
3.6.1.29
polymer
-
Homo sapiens
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.1.4.1
8
9
-
Homo sapiens
3.6.1.29
8.5
-
-
Homo sapiens