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
-
top1-dna
- camp-pde
-
tcf7l2
- milrinone
-
tissue-nonspecific
-
cgmp-inhibited
-
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
results (
results (Engineering
Engineering on EC 3.1.4.1 - phosphodiesterase I
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D392E
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transformation of metal specificity, mutant is a Mn2+-dependent phosphodiesterase/monoesterase
D392N
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transformation of metal and substrate specificity, mutant is a Mn2+-dependent phosphodiesterase
H189A
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transformation of metal and substrate specificity, mutant is a Mn2+-dependent phosphodiesterase
H189D
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transformation of metal and substrate specificity, mutant is a Mn2+-dependent phosphodiesterase. Strong stimulation of activity
H189E
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transformation of substrate specificity, mutant is a Mn2+/Ni2+-dependent phosphodiesterase
H376D
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transformation of metal specificity, mutant is a Mn2+-dependent phosphodiesterase/monoesterase
H376N
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transformation of metal specificity, mutant is a Mn2+-dependent phosphodiesterase/monoesterase
H76A
H263A
H493N
the mutant displays reduced in vitro catalytic activity compared to the wild type enzyme
H493R
K121Q
C57A
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mutant shows severely reduced activity towards p-nitrophenyl phenylphosphonate compared to the wild type enzyme
C57S
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mutant shows reduced activity towards p-nitrophenyl phenylphosphonate compared to the wild type enzyme
H218A
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mutant shows reduced activity towards p-nitrophenyl phenylphosphonate compared to the wild type enzyme
K337A
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mutant shows reduced activity towards p-nitrophenyl phenylphosphonate compared to the wild type enzyme
N78A
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mutant shows reduced activity towards p-nitrophenyl phenylphosphonate compared to the wild type enzyme
Q13A
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mutant shows increased activity towards p-nitrophenyl phenylphosphonate compared to the wild type enzyme
T107A
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mutant shows reduced activity towards p-nitrophenyl phenylphosphonate compared to the wild type enzyme
Y105A
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mutant shows reduced activity towards p-nitrophenyl phenylphosphonate compared to the wild type enzyme
H182A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme, potentiates the cytotoxicity of the Hisgab mutants and induces a DNA topoisomerase 1-independent lethal phenotype in combination with the H432N mutant
H182A/H432N
the mutant protein reveals a dramatic (210fold) reduction in catalytic activity compared to the wild type
H182A/H432R
the mutant protein reveals a dramatic (more than 50%) reduction in catalytic activity compared to the wild type
H182F
H432N
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
H432R
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
H182F
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catalytically inactive mutant, expression of this Tdp1H182F protein does not reveal an enhanced Topo1-dependent toxicity or an increased CPT sensitivity, suggesting that sequestering of the DNA-adduct does not hinder repair by alternative pathways
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additional information
H263A
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the enzyme mutant retains the ability to bind an apurinic/apyrimidinic site-containing DNA, but does not reveal endonuclease activity, it fails to hydrolyze the apurinic/apyrimidinic site
H263A
the mutant displays reduced in vitro catalytic activity compared to the wild type enzyme
H493R
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SCAN1, the enzyme mutant retains the ability to bind an apurinic/apyrimidinic site-containing DNA, but does not reveal endonuclease activity, it fails to hydrolyze the apurinic/apyrimidinic site
H493R
the mutant displays reduced in vitro catalytic activity compared to the wild type enzyme
K121Q
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the mutation does not reveal evidence for association with type 2 diabetic end-stage renal disease in African-Americans
K121Q
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the mutation is closely associated with insulin resistance, type 2 diabetes mellitus, and cardio- and nephrovascular diseases, the product of this polymorphism has a 2-3fold increased binding affinity for the insulin receptor and is more potent than the wild type PC-1 protein
K121Q
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the polymorphism in the ectonucleotide pyrophosphatase/phosphodiesterase-1 gene is associated with insulin resistance, obesity, and hepatitis C viremia and core antigen levels in chronic hepatitis C virus carriers
H182F
catalytically inactive mutant, expression of this Tdp1H182F protein does not reveal an enhanced Topo1-dependent toxicity or an increased CPT sensitivity, suggesting that sequestering of the DNA-adduct does not hinder repair by alternative pathways
additional information
loss-of-function AtTDP mutation , genomic structure of the tdp T-DNA insertion mutant, overview. The tdp Dwarf mutant is caused by reduced cell numbers, phenotype, overview
additional information
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homozygous PiggyBac insertion, c03958, disrupts the 5'-UTR of gene gkt resulting in mutant flies that are defective in hydrolyzing 3'-DNA-tyrosyl residues. The phenotype iss rescued by neuronal expression of the enzyme TDP1
additional information
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mutation of the Msx2 DNA binding site, to prevent binding of Msx2 to this site, inhibits PC-1 promoter activity in FGF2 treated MC3T3E1(C4) calvarial pre-osteoblast cells
additional information
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knocking down TDP1 in cells expressing a dominant negative form of PARP1 and co-silencing of TDP1 and the checkpoint control gene RAD17, overview
additional information
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overexpression and suppression of the enzyme in HCT116 cells, increased alternariol-mediated rate of DNA strand breaks in TDP1-suppressed HCT116 cells
additional information
construction of a series of N-terminal deletion constructs of LdTdp1 with a GFP fused at the C-terminus, expression in Leishmania donovani. This C-terminal deletion construct exhibits cytoplasmic distribution of green fluorescence
additional information
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construction of a series of N-terminal deletion constructs of LdTdp1 with a GFP fused at the C-terminus, expression in Leishmania donovani. This C-terminal deletion construct exhibits cytoplasmic distribution of green fluorescence
additional information
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Pde1c-/- and Pde4a-/- knockout mutants to examine the role of the PDEs in olfactory transduction. Pde1c-/- OSNs (olfactory sensory neuron cilia) show reduced sensitivity and attenuated adaptation to repeated stimulation, suggesting that PDE1C may be involved in regulating sensitivity and adaptation
