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Literature summary for 3.1.4.1 extracted from

  • Ito, K.; Yamamoto, T.; Minamiura, N.
    Phosphodiesterase I in human urine: purification and characterization of the enzyme (1987), J. Biochem., 102, 359-367.
    View publication on PubMed
Search for more literature for 3.1.4.1

General Stability

General Stability Organism
Co2+ stabilizes Homo sapiens
Zn2+ stabilizes Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol inactivation reversed by Zn2+ Homo sapiens
dithiothreitol inactivation reversed by Zn2+ Homo sapiens
EDTA inactivation reversed by Zn2+ to 90% , by Co2+ to 40% , by Ca2+ to 25% Homo sapiens
glutathione
-
 Homo sapiens
L-cysteine inactivation reversed by Zn2+ Homo sapiens
additional information no inhibition by L-ascorbic acid Homo sapiens
Reducing agents inactivation reversed by Zn2+ Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ slight activation Homo sapiens
Co2+ activation Homo sapiens
divalent cations required for activity Homo sapiens
Zn2+ activation Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
190000
-
 gel filtration Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
[nucleotide]n + H2O = [nucleotide]m + nucleotide the enzyme may be able to recognize nucleoside 5'-monophosphates in the substrates and nick them even if the phosphodiester bonds are closed covalently, although the mode of action of this enzyme on oligo- or polynucleotides is typically exonucleolytic Homo sapiens
a

Source Tissue

Source Tissue Comment Organism Textmining
urine
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.08
-
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-p-nitrophenyl deoxythymidine 5'-phosphate + H2O
-
 Homo sapiens 5'-dTMP + p-nitrophenol
-
 ?
ADP + H2O
-
 Homo sapiens AMP + phosphate
-
 ?
ATP + H2O
-
 Homo sapiens 5'-AMP + diphosphate
-
 ?
bis(p-nitrophenyl) phosphate + H2O
-
 Homo sapiens ?
-
 ?
cyclic 3',5'-mononucleotides + H2O phosphodiester bonds Homo sapiens mononucleoside 5'-phosphate
-
 ?
dinucleoside monophosphates + H2O 3'-5' linkage Homo sapiens mononucleoside 5'-phosphate
-
 ?
DNA + H2O enzyme hydolyzes single-stranded DNA more preferentially than double-stranded DNA, the enzyme also hydrolyzes nicked superhelical covalently closed circular phiX174RFI DNA to yield first open circular DNA and then linear DNA Homo sapiens DNA(n-1) + 2'-deoxynucleoside 5'-phosphate
-
 ?
additional information no activity with p-nitrophenylthymidine 3'-phosphate Homo sapiens ?
-
 ?
NAD+ + H2O
-
 Homo sapiens 5'-AMP + NMN
-
 ?
oligonucleotides + H2O specific for 3'-5'-direction from the 3'-hydroxyl terminal in a stepwise manner Homo sapiens oligonucleotides(n-1) + 5'-mononucleotides
-
 ?
poly A + H2O
-
 Homo sapiens 5'-AMP
-
 ?
poly G + H2O
-
 Homo sapiens 5'-GMP
-
 ?
poly U + H2O
-
 Homo sapiens 5'-UMP
-
 ?
polynucleotides + H2O specific for 3'-5'-direction from the 3'-hydroxyl terminal in a stepwise manner Homo sapiens polynucleotides(n-1) + 5'-mononucleotides
-
 ?
RNA + H2O
-
 Homo sapiens RNA(n-1) + nucleoside 5'-phosphate
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 up to, metal-free enzyme is less heat stable than the native enzyme, the stability of the metal-free enzyme is restored to the level of the native enzyme by Zn2+ or Co2+ Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 9.1
-
 Homo sapiens

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 11 stable between Homo sapiens