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

BRENDA support

Literature summary for 3.2.2.27 extracted from

  • Zharkov, D.O.; Mechetin, G.V.; Nevinsky, G.A.
    Uracil-DNA glycosylase: Structural, thermodynamic and kinetic aspects of lesion search and recognition (2010), Mutat. Res., 685, 11-20.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
human UNG gene produces two mRNA and two protein products due to alternative transcription initiation sites Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information UNG mutants with the set of bonds in the conserved 143GQ144 motif optimized for recognition of Cyt or Thy instead of Ura are able to excise normal pyrimidines from DNA and confer a spontaneous mutator phenotype to overexpressing Escherichia coli cells Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
4-methylindole 4-methylindole is an adenine isostere incapable of hydrogen bonding, and its pair with Thy is inherently prone to spontaneous opening, structure of hUNGin a complex with DNA containing a Thy:4-methylindole pair, a DNA mimic, overview Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information thermodynamics of UNG interactions with undamaged and damaged, e.g. 2'-deoxypseudouridine, substrates Escherichia coli
additional information
-
additional information thermodynamics of UNG interactions with undamaged and damaged, e.g. 2'-deoxypseudouridine, substrates Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion the hUNG1 isoform bears a mitochondrial leader peptide on its N-terminus and is imported into mitochondria Homo sapiens 5739
-
nucleus hUNG2 isoform Homo sapiens 5634
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli uracil-DNA glycosylases are ubiquitously found enzymes that hydrolyze the N-glycosidic bond of deoxyuridine, generating from deamination of cytosine, in DNA, UNG enzymes specifically excise Ura bases from both double-stranded and single-stranded DNA with a slight preference for the latter substrate, and shows no activity against normal DNA bases or against uracil in RNA. As potentially mutagenic and deleterious for cell regulation, uracil must be removed from DNA ?
-
?
additional information Homo sapiens uracil-DNA glycosylases are ubiquitously found enzymes that hydrolyze the N-glycosidic bond of deoxyuridine, generating from deamination of cytosine, in DNA, UNG enzymes specifically excise Ura bases from both double-stranded and single-stranded DNA with a slight preference for the latter substrate, and shows no activity against normal DNA bases or against uracil in RNA. As potentially mutagenic and deleterious for cell regulation, uracil must be removed from DNA ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information uracil-DNA glycosylases are ubiquitously found enzymes that hydrolyze the N-glycosidic bond of deoxyuridine, generating from deamination of cytosine, in DNA, UNG enzymes specifically excise Ura bases from both double-stranded and single-stranded DNA with a slight preference for the latter substrate, and shows no activity against normal DNA bases or against uracil in RNA. As potentially mutagenic and deleterious for cell regulation, uracil must be removed from DNA Escherichia coli ?
-
?
additional information uracil-DNA glycosylases are ubiquitously found enzymes that hydrolyze the N-glycosidic bond of deoxyuridine, generating from deamination of cytosine, in DNA, UNG enzymes specifically excise Ura bases from both double-stranded and single-stranded DNA with a slight preference for the latter substrate, and shows no activity against normal DNA bases or against uracil in RNA. As potentially mutagenic and deleterious for cell regulation, uracil must be removed from DNA Homo sapiens ?
-
?
additional information UNG hydrolyzes the N-glycosidic bond of deoxyuridine in DNA. It binds with appreciable affinity to any DNA, mainly due to the interactions with the charged backbone. Search for the lesion by UNG involves random sliding along DNA alternating with dissociation-association events and partial eversion of undamaged bases for initial sampling. DNA in the complex with UNG is highly distorted to allow the extrahelical recognition of uracil, mechanism of uracil search and recognition by UNG, overview Escherichia coli ?
-
?
additional information UNG hydrolyzes the N-glycosidic bond of deoxyuridine in DNA. It binds with appreciable affinity to any DNA, mainly due to the interactions with the charged backbone. Search for the lesion by UNG involves random sliding along DNA alternating with dissociation-association events and partial eversion of undamaged bases for initial sampling. DNA in the complex with UNG is highly distorted to allow the extrahelical recognition of uracil, mechanism of uracil search and recognition by UNG, structure-function relationship, overview Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More the structural fold of UNG proteins is based on four beta-sheets sandwiched between two pairs of alpha-helices, the surface of the protein globule is traversed by a shallow and narrow positively charged groove, where substrate DNA binds. This groove harbors the enzyme's active site, which in turn contains a deep pocket that accommodates the uracil base, conformational change upon substrate binding, overall structure and conserved structural motifs, structure-function relationship, overview Escherichia coli
More the structural fold of UNG proteins is based on four beta-sheets sandwiched between two pairs of alpha-helices, the surface of the protein globule is traversed by a shallow and narrow positively charged groove, where substrate DNA binds. This groove harbors the enzyme's active site, which in turn contains a deep pocket that accommodates the uracil base, conformational change upon substrate binding, overall structure and conserved structural motifs, structure-function relationship, overview Homo sapiens

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the family I uracil-DNA glycosylases Escherichia coli
More the enzyme belongs to the family I uracil-DNA glycosylases Homo sapiens
UNG
-
Escherichia coli
UNG
-
Homo sapiens
uracil-DNA N-glycosylase
-
Escherichia coli
uracil-DNA N-glycosylase
-
Homo sapiens