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Literature summary for 3.1.4.1 extracted from

  • Lebedeva, N.A.; Rechkunova, N.I.; El-Khamisy, S.F.; Lavrik, O.I.
    Tyrosyl-DNA phosphodiesterase 1 initiates repair of apurinic/apyrimidinic sites (2012), Biochimie, 94, 1749-1753.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged wild-type and mutant enzymes Homo sapiens

Protein Variants

Protein Variants Comment Organism
H263A 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 Homo sapiens
H493R 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 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of enzyme cleavage activity on different apurinic/apyrimidinic-DNA substrates., overview Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens 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 ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes byy nickel affinity and phosphocellulose adsorption chromatography, and for the wild-type enzyme further by gel filtration and heparin affinity chromatography, to homogeneity Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 Homo sapiens ?
-
?
additional information efficiency of apurinic/apyrimidinic site hydrolysis catalyzed by the enzyme decreases in the order: dsAP-DNA/bubble > ssAP-DNA > dsAP-DNA/Flu >> dsAP-DNA, the enzyme shows preference for 3'-substituent located on the termini of DNA compared to nicks Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
TDP1
-
Homo sapiens
tyrosyl-DNA phosphodiesterase 1
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens

General Information

General Information Comment Organism
malfunction whilst the enzyme mutants H493R (SCAN1) and H263A retain the ability to bind an apurinic/apyrimidinic site-containing DNA, both mutants do not reveal endonuclease activity Homo sapiens
physiological function human tyrosyl-DNA phosphodiesterase 1 catalyzes the apurinic/apyrimidinic site cleavage reaction to generate breaks with the 3'- and 5'-phosphate termini. The enzyme activity can contribute to the repair of apurinic/apyrimidinic sites particularly in DNA structures containing ssDNA region or apurinic/apyrimidinic sites in the context of clustered DNA lesions Homo sapiens