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Literature summary for 4.2.99.18 extracted from

  • Kuznetsov, N.A.; Kladova, O.A.; Kuznetsova, A.A.; Ishchenko, A.A.; Saparbaev, M.K.; Zharkov, D.O.; Fedorova, O.S.
    Conformational dynamics of DNA repair by Escherichia coli endonuclease III (2015), J. Biol. Chem., 290, 14338-14349 .
    View publication on PubMedView publication on EuropePMC
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information pre-steady-state kinetic analysis of structural rearrangements of the DNA substrates and uncleavable ligands during their interaction with Endo III Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli Escherichia coli endonuclease III is a DNA glycosylase with a broad substrate specificity for oxidized or reduced pyrimidine bases. Endo III possesses two types of activities: N-glycosylase (hydrolysis of the N-glycosidic bond) and AP lyase (elimination of the 3'-phosphate of the AP-site) ?
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AB83
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Escherichia coli endonuclease III is a DNA glycosylase with a broad substrate specificity for oxidized or reduced pyrimidine bases. Endo III possesses two types of activities: N-glycosylase (hydrolysis of the N-glycosidic bond) and AP lyase (elimination of the 3'-phosphate of the AP-site) Escherichia coli ?
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 ?
additional information analysis of structural rearrangements of the DNA substrates and uncleavable ligands during their interaction with Endo III using oligonucleotide duplexes containing 5,6-dihydrouracil, a natural abasic site, its tetrahydrofuran analogue, and undamaged duplexes carried fluorescent DNA base analogues 2-aminopurine and 1,3-diaza-2-oxophenoxazine as environment-sensitive reporter groups, pre-steady-state kinetic analysis, overview. Endo III induces several fast sequential conformational changes in DNA during binding, lesion recognition, and adjustment to a catalytically competent conformation. The glycosylase uses a multistep mechanism of damage recognition, which likely involves Gln41 and Leu81 as DNA lesion sensors Escherichia coli ?
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 ?

Synonyms

Synonyms Comment Organism
Endo III
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 Escherichia coli
endonuclease III
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 Escherichia coli
Nth
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

General Information

General Information Comment Organism
evolution endonuclease III belongs to the DNA glycosylases of the helix-hairpin-helix-GPD structural superfamily Escherichia coli
additional information endonuclease III uses a multistep mechanism of damage recognition, which likely involves Gln41 and Leu81 as lesion sensors. The principal amino acids involved in the catalysis are Lys120 and Asp138. The former is the nucleophile that attacks the C1' atom of deoxyribose, resulting in the cleavage of the N-glycosydic bond and subsequent formation of a Schiff base covalent intermediate. The following beta-elimination reaction leads to the departure of the 3'-phosphate. The subsequent Schiff base hydrolysis releases the enzyme and leads to formation of a single-strand break in DNA duplex with an alpha/beta-unsaturated aldehyde at the 3'-end and a phosphate at the 5'-end Escherichia coli
physiological function Endonuclease III (Endo III) is a bifunctional DNA glycosylase possessing N-glycosylase and AP lyase activities. Endonuclease III is responsible for base excision repair of oxidized or reduced pyrimidine bases Escherichia coli