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Information on EC 4.2.99.18 - DNA-(apurinic or apyrimidinic site) lyase

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.99 Other carbon-oxygen lyases
                4.2.99.18 DNA-(apurinic or apyrimidinic site) lyase
IUBMB Comments
'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. This group of enzymes was previously listed as endonucleases, under EC 3.1.25.2.
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UNIPROT: O29675
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Synonyms
ap endonuclease, ref-1, ape1/ref-1, apex1, ape/ref-1, apurinic/apyrimidinic endonuclease 1, ap lyase, ape-1, alkbh1, endo iii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AP endonuclease
exonuclease III (ExoIII)
apurinic/apyrimidinic endonuclease
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AP 1
-
-
-
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AP Dnase
-
-
-
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AP endo
-
-
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AP endonuclease
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-
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AP endonuclease Class I
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-
-
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AP lyase
-
-
-
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AP-endonuclease
-
-
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Ape
-
-
-
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APEN
-
-
-
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APEX nuclease
-
-
-
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APN1
-
-
-
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apurinic DNA endonuclease
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-
-
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apurinic endodeoxyribonuclease
-
-
-
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apurinic endonuclease
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-
-
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apurinic-apyrimidinic DNA endonuclease
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-
-
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apurinic-apyrimidinic endodeoxyribonuclease
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-
-
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apurinic-apyrimidinic endonuclease
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-
-
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apurinic/apyrimidinic lyase
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-
-
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apurinic/apyrimidinic specific endonuclease
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-
-
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apyrimidinic endonuclease
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-
-
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class II apurinic/apyrimidinic(AP)-endonuclease
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deoxyribonuclease (apurinic or apyrimidinic)
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-
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E. coli endonuclease III
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-
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endodeoxyribonuclease
-
-
-
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endodeoxyribonuclease III
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-
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endonuclease III
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-
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endonuclease VI
-
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Escherichia coli endonuclease III
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-
-
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HAP1
-
-
-
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HAP1h
-
-
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Micrococcus luteus UV endonuclease
-
-
-
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MMH
-
-
-
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Nfo
-
-
-
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Ntg1p
-
-
-
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Ntg2p
-
-
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NTH1
-
-
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nuclease, apurinic endodeoxyribo-
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nuclease, apurinic-apyrimidinic endodeoxyribo-
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nuclease, endodeoxyribo-, III
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phage-T4 UV endonuclease
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REF-1 protein
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Ref1
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UV endo V
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UV endonuclease
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UV endonuclease V
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SYSTEMATIC NAME
IUBMB Comments
DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase
'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. This group of enzymes was previously listed as endonucleases, under EC 3.1.25.2.
CAS REGISTRY NUMBER
COMMENTARY hide
60184-90-9
-
61811-29-8
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
O29675_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
257
0
29757
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
V217G variant is crystallized with decamer dsDNA molecule, and the three-dimensional structure is determined to 1.7 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F200S
site-directed mutagenesis, by expanding the size of the binding pocket the unspecific endonucleolytic activity is increased
F200S/W215S
site-directed mutagenesis, by expanding the size of the binding pocket the unspecific endonucleolytic activity is increased
V217G
site-directed mutagenesis, by expanding the size of the binding pocket the unspecific endonucleolytic activity is increased
W215S
site-directed mutagenesis, by expanding the size of the binding pocket the unspecific endonucleolytic activity is increased
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
is frequently used in gene technology due to its strong exonucleolytic activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schmiedel, R.; Kuettner, E.B.; Keim, A.; Straeter, N.; Greiner-Stoeffele, T.
Structure and function of the abasic site specificity pocket of an AP endonuclease from Archaeoglobus fulgidus
DNA Repair
8
219-231
2009
Archaeoglobus fulgidus (O29675), Archaeoglobus fulgidus
Manually annotated by BRENDA team