3.1.4.1: phosphodiesterase I
This is an abbreviated version!
For detailed information about phosphodiesterase I, go to the full flat file.
Word Map on EC 3.1.4.1
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3.1.4.1
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camp
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phosphodiesterases
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calcification
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arterial
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topoisomerase
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rolipram
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monophosphate
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camp-specific
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infancy
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osteoblast
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hypophosphatemic
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rickets
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camptothecin
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pseudoxanthoma
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ectoenzyme
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topotecan
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5'-nucleotide
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elasticum
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ibmx
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ankylosis
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3'-phosphate
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zaprinast
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top1-dna
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camp-pde
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tcf7l2
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milrinone
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qq
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tissue-nonspecific
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cgmp-inhibited
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cgmp-stimulated
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pyrophosphohydrolase
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cilomilast
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cementum
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3-isobutyl-1-methylxanthine
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rolipram-sensitive
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vinpocetine
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cardiotonic
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pharmacology
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medicine
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synthesis
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drug development
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biotechnology
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analysis
- 3.1.4.1
- camp
- phosphodiesterases
- calcification
- arterial
-
topoisomerase
- rolipram
- monophosphate
-
camp-specific
-
infancy
- osteoblast
-
hypophosphatemic
- rickets
- camptothecin
-
pseudoxanthoma
-
ectoenzyme
- topotecan
-
5'-nucleotide
- elasticum
- ibmx
- ankylosis
- 3'-phosphate
- zaprinast
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top1-dna
- camp-pde
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tcf7l2
- milrinone
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tissue-nonspecific
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cgmp-inhibited
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cgmp-stimulated
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pyrophosphohydrolase
- cilomilast
-
cementum
- 3-isobutyl-1-methylxanthine
-
rolipram-sensitive
- vinpocetine
-
cardiotonic
- pharmacology
- medicine
- synthesis
- drug development
- biotechnology
- analysis
Reaction
Synonyms
5' nucleotide phosphodiesterase/alkaline phosphodiesterase I, 5'-exonuclease, 5'-NPDase, 5'-nucleotide phosphodiesterase, 5'-PDase, 5'-PDE, 5'-phosphodiesterase, 5'NPDE, alkaline phosphodiesterase, Ap3A (Ap4A) hydrolase, autotaxin, B10, calcium-dependent phosphodiesterase 1C, cleavage/polyadenylation specificity factor, CPSF-73, cRNPMase-5'-PDase, cyclic nucleotide phosphodiesterase 1, cyclic-ribonucleotide phosphomutase-5'-phosphodiesterase I, ecto-NPPase, ecto-nucleotide pyrophosphatase/phosphodiesterase 1, ectonucleotide pyrophosphatase phosphodiesterase 1, ectonucleotide pyrophosphatase/phosphodiesterase 1, ectonucleotide pyrophosphate/phosphodiesterase-1, ENPP-1, ENPP1, exonuclease I, exophosphodiesterase, gp130RB13-6, liver alkaline phosphodiesterase 1, liver nucleotide phosphodiesterase, More, NPP, NPP-1, NPP/PDE, NPP1, NPP2, NPP3, nucleotide phosphodiesterase, nucleotide phosphodiesterase/pyrophosphatase, nucleotide pyrophosphatase/alkaline phosphodiesterase I, nucleotide pyrophosphatase/phosphodiesterase 1, nucleotide pyrophosphatase/phosphodiesterase I, nucleotide pyrophosphatase/phosphodiesterase-1, nucleotide pyrophosphatase/phosphodiesterase-2, nucleotide pyrophosphatase/phosphodiesterase-3, orthophosphoric diester phosphohydrolase, PC-1, PDase, PDE, PDE 1A, PDE I, PDE1, PDE1A, PDE1C, PDE4A, PDEase, phosphodiesterase, phosphodiesterase 1, phosphodiesterase 1A, phosphodiesterase 1C, phosphonate monoester hydrolase/phosphodiesterase, phosphoric diester hydrolase, plant exonuclease I, plasma cell antigen 1, plasma cell membrane glycoprotein, plasma cell membrane protein-1, PMH, RNase J1, SMPDL3A, sphingomyelin phosphodiesterase, acid-like 3A, SVPD, Tdp 1, TDP1, tRNase Z, tyrosyl DNA phosphodiesterase 1, tyrosyl-DNA phosphodiesterase 1, tyrosyl-DNA phosphodiesterase I, tyrosyl-DNA-phosphodiesterase I, yfcE
ECTree
3.1.4.1 phosphodiesterase IAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.1.4.1 - phosphodiesterase I
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-phosphohistidyl-linked tyrosyl-DNA phosphodiesterase I-DNA complex + H2O
?
tyrosyl-DNA phosphodiesterase I hydrolyzes the 3'phospho-histidyl bond formed between tyrosyl-DNA phosphodiesterase I and DNA
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?
3'-phosphotyrosyl-linked topoisomerase I-DNA complex + H2O
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tyrosyl-DNA phosphodiesterase I hydrolyzes the 3'phospho-tyrosyl bond formed between DNA topoisomerase I and DNA
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?
5'-phosphotyrosyl-linked topoisomerase II-DNA complex + H2O
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tyrosyl-DNA phosphodiesterase I hydrolyzes the 5'phospho-tyrosyl bond formed between DNA topoisomerase II and DNA
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?
diadenosine polyphosphate + H2O
AMP + adenosine polyphosphate-1
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phosphodiesterase can be considered as a catabolic enzyme
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diadenosine polyphosphate + H2O
AMP + adenosine polyphosphate-1
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phosphodiesterase can be considered as a catabolic enzyme
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?
additional information
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AtTDP has Tyr-phosphodiesterase activity for the topoisomerase-DNA complex
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?
additional information
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the enzyme may be important in nucleotide metabolism on the cell surface
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?
additional information
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E2REL5
substrates are protein-DNA adducts, such as camptothecin stabilized Topo1-DNA adducts, and modified nucleotides, including oxidized nucleotides and chain terminating nucleoside analogues
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?
additional information
?
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substrates are protein-DNA adducts, such as camptothecin stabilized Topo1-DNA adducts, and modified nucleotides, including oxidized nucleotides and chain terminating nucleoside analogues
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?
additional information
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substrates are protein-DNA adducts, such as camptothecin stabilized Topo1-DNA adducts, and modified nucleotides, including oxidized nucleotides and chain terminating nucleoside analogues
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?
additional information
?
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PC-1, PC-1 may take part in purine uptake for metabolic needs of cells
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?
additional information
?
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enzyme might function as a modulating factor of platelet aggregation
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?
additional information
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enzyme may be involved in nucleotides metabolism in human plasma
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?
additional information
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PC-1 plays a major role in bone and cartilage metabolism by producing diphosphate
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?
additional information
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tyrosyl-DNA phosphodiesterase 1 catalyses the hydrolysis of phosphodiester linkages between a DNA 3' phosphate and a tyrosine residue as well as a variety of other DNA 3 substituents, the enzyme shows affinity for the substrate increased as the DNA length
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?
additional information
?
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SMPDL3A is a functional metallophosphoesterase, and despite having no detectable activity towards sphingomyelin, possesses a nucleotide phosphodiesterase activity, particularly strongly against nucleotide triphosphates
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?
additional information
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SMPDL3A is a functional metallophosphoesterase, and despite having no detectable activity towards sphingomyelin, possesses a nucleotide phosphodiesterase activity, particularly strongly against nucleotide triphosphates
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?
additional information
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substrates are protein-DNA adducts, such as camptothecin stabilized Topo1-DNA adducts, and modified nucleotides, including oxidized nucleotides and chain terminating nucleoside analogues, substrates vary in size and complexity
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?
additional information
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the enzyme catalyzes the hydrolysis of 3' phosphotyrosyl linkers and other 3'-end blocking lesions. When Top1 nicks double-stranded DNA, a covalent cleavage complex is formed that can be repaired by the enzyme, the mechanism involves the following steps: first, as Lys265 and Lys495 residues in the catalytic site coordinate the oxygen atoms of the phosphate group, His263 attacks the phosphorus atom linked to the oxygen of the Top1 catalytic residue, Tyr723, at the 3' end of DNA. Second, the TDP1-DNA covalent intermediate formed is hydrolyzed by a His493-activated water molecule, leading to the generation of a DNA product with a 3' phosphate
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?
additional information
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the enzyme cleaves the apurinic/apyrimidinic site in DNA by hydrolysis of the phosphodiester bond between the substituent and 5' adjacent phosphate. The product of enzyme cleavage in the case of the apurinic/apyrimidinic site is unstable and is hydrolyzed with the formation of 3'- and 5'-margin phosphates. The following repair demands the ordered action of polynucleotide kinase phosphorylase, with XRCC1, DNA polymerase beta, and DNA ligase, mechanism, overview
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additional information
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tyrosyl-DNA phosphodiesterase 1 catalyzes the hydrolysis of the phosphodiester linkage between the DNA 3'-phosphate and a tyrosine residue as well as a variety of other DNA 30 damaged termini. The enzyme can liberate the 3'-DNA phosphate termini from apurinic/apyrimidinic sites. The enzyme is more active in the cleavage of the apurinic/apyrimidinic sites inside bubble-DNA structure in comparison to ssDNA containing apurinic/apyrimidinic site, it hydrolyzes apurinic/apyrimidinic sites opposite to bulky fluorescein adduct faster than apurinic/apyrimidinic sites located in dsDNA, specificity of the apurinic/apyrimidinic site cleavage activity
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additional information
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tyrosyl-DNA phosphodiesterase I specifically catalyzes the hydrolysis of the phosphodiester bond between the catalytic Tyr723 of Top1 and DNA-3'-phosphate, then polynucleotide kinase phosphatase hydrolyzes the resulting 3'-phosphate end and catalyzes the phosphorylation of the 5'-hydroxyl end of the broken DNA strand. This results in a broken DNA strand with termini consisting of a 5'-phosphate and 3'-hydroxyl for DNA repair. DNA polymerase beta replaces the missing DNA segment, and finally DNA ligase III reseals the broken DNA
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?
additional information
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the enzyme cleaves the 3'-diester bond between tyrosine and DNA as well as removes other lesions, producing a 3'-phosphate that can be removed by polynucleotide kinase/phosphatase
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?
additional information
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the enzyme hydrolyzes the phosphodiester bond between a catalytic tyrosine Tyr723 (human) of topoisomerase 1 and DNA 3'-phosphate
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?
additional information
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the physiological function of PDE in plant cell is presumably the degradation of nucleic acids
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?
additional information
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implication of enzyme in intra- and extracellular processes, overview
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?
additional information
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PC-1, PC-1 may take part in purine uptake for metabolic needs of cells
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?
additional information
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PC-1, PC-1 may take part in purine uptake for metabolic needs of cells
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?
additional information
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PC-1, nucleotide pyrophosphatase/alkaline phosphodiesterase I, may have a role in the regulation of N-linked glycosylation, it may regulate the availability of nucleotide sugar precusors at the site of oligosaccharide synthesis
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?
additional information
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substrates are protein-DNA adducts, such as camptothecin stabilized Topo1-DNA adducts, and modified nucleotides, including oxidized nucleotides and chain terminating nucleoside analogues
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?
additional information
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PC-1, nucleotide pyrophosphatase/alkaline phosphodiesterase I, may have a role in the regulation of N-linked glycosylation, it may regulate the availability of nucleotide sugar precusors at the site of oligosaccharide synthesis
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?
additional information
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NPP1 exhibits hydrolytic activity toward ADP-glucose and plastid-targeting ability
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?
additional information
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NPP1 exhibits hydrolytic activity toward ADP-glucose and plastid-targeting ability
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?
additional information
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unlike isozyme NPP1, isozyme NPP3 exhibits no hydrolytic activity toward ADP-glucose and no plastid-targeting ability
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?
additional information
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unlike isozyme NPP1, isozyme NPP3 exhibits no hydrolytic activity toward ADP-glucose and no plastid-targeting ability
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?
additional information
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phosphodiesterase activity results in the cleavage of nucleotides from nucleic acids and thus may be involved in catabolism of extracellular DNA. Essential function may be to hydrolyze polyribo- and polydeoxyribonucleotides. The enzyme may be important in cell differentiation during carcinogenesis
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additional information
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PC-1, plasma-membrane-associated enzyme with nucleotide pyrophosphatase/phosphodiesterase I activity is probably involved in the clearance of extracellular nucleotides such as ATP and diadenosine polyphosphates
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?
additional information
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isoform NPP1 is involved in cleavage of extracellular diadenosine polyphosphates in brain
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?
additional information
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substrates are protein-DNA adducts, such as camptothecin stabilized Topo1-DNA adducts, and modified nucleotides, including oxidized nucleotides and chain terminating nucleoside analogues
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?
additional information
?
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substrates are protein-DNA adducts, such as camptothecin stabilized Topo1-DNA adducts, and modified nucleotides, including oxidized nucleotides and chain terminating nucleoside analogues, substrates vary in size and complexity
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?
additional information
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the enzyme hydrolyzes the covalent bond between the tyrosyl residue of topoisomerase 1 and the 3'-phosphate group in DNA. The enzyme is able to initiate the cleavage of internal apurinic/apyrimidinic sites or 3-hydroxy-2-hydroxymethyl tetrahydrofuran in DNA and its subsequent repair
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?
additional information
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the enzyme hydrolyzes the covalent bond between the tyrosyl residue of topoisomerase 1 and the 3'-phosphate group in DNA. The enzyme is able to initiate the cleavage of internal apurinic/apyrimidinic sites or 3-hydroxy-2-hydroxymethyl tetrahydrofuran in DNA and its subsequent repair
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?
additional information
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substrates are protein-DNA adducts, such as camptothecin stabilized Topo1-DNA adducts, and modified nucleotides, including oxidized nucleotides and chain terminating nucleoside analogues, substrates vary in size and complexity
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?
