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Literature summary extracted from

  • Luthje, J.; Ogilvie, A.
    Catabolism of Ap3A and Ap4A in human plasma. Purification and characterization of a glycoprotein complex with 5'-nucleotide phosphodiesterase activity (1985), Eur. J. Biochem., 149, 119-127.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment 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 Comment 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 Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment 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 Homo sapiens
3.1.4.1 Zn2+ 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] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.1 diadenosine polyphosphate + H2O Homo sapiens phosphodiesterase can be considered as a catabolic enzyme AMP + adenosine polyphosphate-1
-
?
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 UniProt Comment Textmining
3.1.4.1 Homo sapiens
-
-
-
3.6.1.29 Homo sapiens
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.4.1 glycoprotein
-
Homo sapiens
3.6.1.29 glycoprotein mannoside Homo sapiens

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.4.1
-
Homo sapiens

Source Tissue

EC Number Source Tissue Comment 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 [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.4.1 additional information
-
-
Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.1 adenosine 5'-P1-tetraphospho-P4-5'''-adenosine + H2O
-
Homo sapiens AMP + ATP
-
?
3.1.4.1 ATP + H2O
-
Homo sapiens 5'-AMP + diphosphate
-
?
3.1.4.1 diadenosine 5',5'''-P1,P3-triphosphate + H2O
-
Homo sapiens AMP + ADP
-
?
3.1.4.1 diadenosine polyphosphate + H2O phosphodiesterase can be considered as a catabolic enzyme Homo sapiens AMP + adenosine polyphosphate-1
-
?
3.1.4.1 dinucleotides + H2O
-
Homo sapiens ?
-
?
3.1.4.1 additional information no activity with p-nitrophenylthymidine 3'-phosphate Homo sapiens ?
-
?
3.1.4.1 additional information broad substrate specificity Homo sapiens ?
-
?
3.1.4.1 additional information enzyme might function as a modulating factor of platelet aggregation Homo sapiens ?
-
?
3.1.4.1 NAD+ + H2O
-
Homo sapiens 5'-AMP + NMN
-
?
3.1.4.1 p-nitrophenylthymidine 5'-phosphate + H2O
-
Homo sapiens 5'-TMP + p-nitrophenol
-
?
3.1.4.1 UTP + H2O
-
Homo sapiens UMP + diphosphate
-
?
3.6.1.29 Ap4A + H2O
-
Homo sapiens ?
-
?
3.6.1.29 ATP + 2 H2O
-
Homo sapiens AMP + 2 phosphate
-
?
3.6.1.29 diadenosine 5',5''-P1,P4-tetraphosphate + H2O
-
Homo sapiens AMP + ATP
-
?
3.6.1.29 NAD+ + H2O
-
Homo sapiens ?
-
?
3.6.1.29 P1-P3-bis(5'-adenosyl) triphosphate + H2O
-
Homo sapiens ADP + AMP
-
?
3.6.1.29 thymidine 5'-monophosphate p-nitrophenylester + H2O
-
Homo sapiens ?
-
?
3.6.1.29 UTP + 2 H2O
-
Homo sapiens UMP + 2 phosphate
-
?

Subunits

EC Number Subunits Comment 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

Synonyms

EC Number Synonyms Comment Organism
3.1.4.1 Ap3A (Ap4A) hydrolase
-
Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.4.1 8 9
-
Homo sapiens
3.6.1.29 8.5
-
-
Homo sapiens