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Information on EC 3.2.2.27 - uracil-DNA glycosylase

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.27 uracil-DNA glycosylase
IUBMB Comments
Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. EC 3.2.2.27 and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA.
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UNIPROT: Q58829
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Hydrolyses single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil
Synonyms
uracil-dna glycosylase, smug1, dna n-glycosylase, ung-1, ul114, uracil dna-glycosylase, uracil-dna n-glycosylase, uracil dna glycosylase 2, thd1p, mjudg, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
uracil-DNA deoxyribohydrolase (uracil-releasing)
Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. EC 3.2.2.27 and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA.
CAS REGISTRY NUMBER
COMMENTARY hide
59088-21-0
cf. EC 3.2.2.28
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
8-oxoguanine-mismatched double-stranded DNA + H2O
8-oxoguanine + double-stranded DNA with abasic site
show the reaction diagram
the enzyme effciently removes uracil from both single- and double-stranded DNA. Activity with oligonucleotide duplexes containing 8-oxoguanine is 5fold lower than that of oligonucleotide duplex containing U:T
-
-
?
8-oxoguanine-mismatched single-stranded DNA + H2O
8-oxoguanine + single-stranded DNA with abasic site
show the reaction diagram
the enzyme effciently removes uracil from both single- and double-stranded DNA
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
show the reaction diagram
uracil-mismatched double-stranded oligonucleotide + H2O
uracil + double-stranded oligonucleotide with abasic site
show the reaction diagram
oligonucleotide duplex containing a U:T mispair
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
show the reaction diagram
the enzyme effciently removes uracil from both single- and double-stranded DNA
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
show the reaction diagram
cytosine bases can be deaminated spontaneously to uracil, causing DNA damage. Uracil-DNA glycosylase repairs this kind of DNA damage
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron-sulfur cluster
the [4Fe-4S]-binding cluster is important for the DNA binding and catalytic activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 65
the enzyme is more active at 65°C than at 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Y1434_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
220
0
25938
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D150E
displays reduced activity of about 70% of the wild type value
D150W
completely lacks DNA glycosylase activity
E132K
mutation converts the enzyme into a bifunctional glycosylase/AP lyase capable of both removing uracil at a glycosylic bond and cleaving the phosphodiester backbone at an apurinic/apyrimidinic site. The mutant catalyzes a beta-elimination reaction at the apurinic/apyrimidinic site via uracil excision and forms a Schiff base intermediate in the form of a protein-DNA complex
Y152E
retains unchanged levels of uracil-DNA glycosylase activity
Y152N
retains unchanged levels of uracil-DNA glycosylase activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Im, E.K.; Han, Y.S.; Chung, J.H.
Functional changes in a novel uracil-DNA glycosylase determined by mutational analyses
Mikrobiologiia
77
644-650
2008
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii (Q58829), Methanocaldococcus jannaschii DSM 2661 (Q58829)
Manually annotated by BRENDA team
Chung, J.H.; Im, E.K.; Park, H.Y.; Kwon, J.H.; Lee, S.; Oh, J.; Hwang, K.C.; Lee, J.H.; Jang, Y.
A novel uracil-DNA glycosylase family related to the helix-hairpin-helix DNA glycosylase superfamily
Nucleic Acids Res.
31
2045-2055
2003
Methanocaldococcus jannaschii (Q58829), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58829)
Manually annotated by BRENDA team