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Literature summary for 3.1.21.2 extracted from

  • Golan, G.; Ishchenko, A.; Khassenov, B.; Shoham, G.; Saparbaev, M.
    Coupling of the nucleotide incision and 3'-5' exonuclease activities in Escherichia coli endonuclease IV: Structural and genetic evidences (2010), Mutat. Res., 685, 70-79.
    View publication on PubMed
Search for more literature for 3.1.21.2

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type enzyme and mutant H69A, hanging-drop vapor diffusion method, mxing of 0.0015 ml of protein solution containing 10 mg/ml protein with 0.002 ml of reservoir solution containing 35% PEG 400 and 100 mM HEPES, pH 5.5, 20°C, 7 days, X-ray diffraction structure determination and analysis at 1.55 A resolution Escherichia coli

Protein Variants

Protein Variants Comment Organism
G149D site-directed mutagenesis, the mutant is deficient in both nucleotide incision repair and exonuclease activities Escherichia coli
H69A site-directed mutagenesis, the mutant is deficient in both nucleotide incision repair and exonuclease activities. The crystal structure of Nfo-H69A mutant reveals the loss of one of the active site zinc atoms and rearrangements of the catalytic site, but no gross changes in the overall enzyme conformation Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000025
-
 21-mer C-Grec wild-type enzyme, pH 7.6, 37°C Escherichia coli
0.0000272
-
 21-mer C-Grec mutant H69A, pH 7.6, 37°C, in presence of Zn2+ Escherichia coli
0.000028
-
 21-mer C-Grec mutant G149D, pH 7.6, 37°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ dependent on Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli Nfo-catalyzed nucleotide incision repair and exonuclease activities can generate a single-strand gap at the 5' side of 5,6-dihydrouracil residue ?
-
 ?
additional information Escherichia coli AB1157 Nfo-catalyzed nucleotide incision repair and exonuclease activities can generate a single-strand gap at the 5' side of 5,6-dihydrouracil residue ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene nfo
-
Escherichia coli AB1157
-
 gene nfo
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
21-mer C-Grec + H2O
-
 Escherichia coli ?
-
 ?
21-mer C-Grec + H2O
-
 Escherichia coli AB1157 ?
-
 ?
additional information Nfo-catalyzed nucleotide incision repair and exonuclease activities can generate a single-strand gap at the 5' side of 5,6-dihydrouracil residue Escherichia coli ?
-
 ?
additional information Nfo-catalyzed nucleotide incision repair and exonuclease activities can generate a single-strand gap at the 5' side of 5,6-dihydrouracil residue Escherichia coli AB1157 ?
-
 ?

Synonyms

Synonyms Comment Organism
apurinic/apyrimidinic endonuclease
-
 Escherichia coli
endonuclease IV
-
 Escherichia coli
Nfo
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0003
-
 21-mer C Grec mutant H69A, pH 7.6, 37°C, in presence of Zn2+ Escherichia coli
0.0088
-
 21-mer C Grec mutant G149D, pH 7.6, 37°C Escherichia coli
0.28
-
 21-mer C Grec wild-type enzyme, pH 7.6, 37°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Escherichia coli

General Information

General Information Comment Organism
additional information Nfo catalyzed nucleotide incision and 3'-5' exonuclease activities are genetically coupled. modeling of nucleotide incision coupled to 3'-5' exonuclease activity preventing formation of lethal double-strand breaks when repairing bi-stranded clustered DNA damage, overview Escherichia coli
physiological function in the nucleotide incision repair pathway, an apurinic/apyrimidinic endonuclease incises duplex DNA 5' next to oxidatively damaged nucleotide. The multifunctional Escherichia coli endonuclease IV is involved in both base excision repair and nucleotide incision repair pathways, overview Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.012
-
 21-mer C Grec mutant H69A, pH 7.6, 37°C, in presence of Zn2+ Escherichia coli
0.317
-
 21-mer C Grec mutant G149D, pH 7.6, 37°C Escherichia coli
8
-
 21-mer C Grec wild-type enzyme, pH 7.6, 37°C Escherichia coli