Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.99.B1 extracted from

  • Grin, I.R.; Khodyreva, S.N.; Nevinsky, G.A.; Zharkov, D.O.
    Deoxyribophosphate lyase activity of mammalian endonuclease VIII-like proteins (2006), FEBS Lett., 580, 4916-4922.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli and purified Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00021
-
25-mer-deoxyoligonucleotide 3'-labeled uracil-containing DNA duplex NEIL1 Mus musculus
0.0022
-
25-mer-deoxyoligonucleotide 3'-labeled uracil-containing DNA duplex NEIL2 Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no effect my the presence or the absence of Mg2+. The activity of NEIL1 and NEIL2 are similar in potassium phosphate and Tris-HCl buffer Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38200
-
NEIL2, protein part of the enzyme-DNA complex, when trapped by the addition of NaBH4 to the dRP lyase activity assay. NaBH4 reduces the Schiff base formed between the catalytic nucleophile of dRP lyase and C1' of the dRP site Mus musculus
43500
-
NEIL1, protein part of the enzyme-DNA complex, when trapped by the addition of NaBH4 to the dRP lyase activity assay. NaBH4 reduces the Schiff base formed between the catalytic nucleophile of dRP lyase and C1' of the dRP site Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Mus musculus

Reaction

Reaction Comment Organism Reaction ID
catalysis of the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site in DNA where a DNA-(apurinic or apyrimidinic site) lyase has already cleaved the C-O-P bond 3' to the apurinic or apyrimidinic site NEIL1 and NEIL2 are capable of removing 2-deoxyribose 5-phosphate from DNA with the effiency comparable to that of Polbeta, and they can substitute for Polbeta dRPase activity in a reconstituted base excision repair (BER) system Mus musculus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
NEIL1 and NEIL2 show similar efficiency, when A, C, or T are replaced opposite the lesion, and the excision opposite G was 1.5-2fold lower Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
25-mer-deoxyoligonucleotide 3'-labeled uracil-containing DNA duplex [32P]-labeled substarte, treated with uracil-DNA glycosylase and apurinic/apyrimidinic endonuclease Mus musculus ? + 2-deoxy-D-ribose 5-phosphate the products are stabilized by NaBH4 reduction of the Schiff base, formed between the catalytic nucleophile of the dRP lyase and C1' of rhe 2-deoxyribose 5-phosphate site, verifying the dRP removal by a beta-elimination ?

Synonyms

Synonyms Comment Organism
deoxyribo-5'-phosphate lyase
-
Mus musculus
dRP lyase
-
Mus musculus
dRPase
-
Mus musculus
mammalian endonuclease VIII-like protein
-
Mus musculus
NEIL1
-
Mus musculus
NEIL2
-
Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Mus musculus