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Information on EC 4.2.99.18 - DNA-(apurinic or apyrimidinic site) lyase and Organism(s) Bos taurus and UniProt Accession P23196
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4.2.99.18 DNA-(apurinic or apyrimidinic site) lyaseIUBMB 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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Word Map
- 4.2.99.18
- strand
-
exonuclease
- glycosylases
-
single-stranded
- pyrimidine
- endonucleases
- 8-oxoguanine
- nick
- thymine
- uracil
- duplex
-
genotoxic
- xrcc1
-
phosphodiester
- comet
- deoxyribose
- methanesulfonate
- mispairs
-
uracil-dna
-
depurinated
-
beta-elimination
-
excise
- formamidopyrimidine
-
3'-phosphatase
- 7,8-dihydro-8-oxoguanine
- tetrahydrofuran
-
site-containing
-
mutyh
-
endonucleolytic
-
xeroderma
- pigmentosum
-
base-excision
- 3'-phosphodiesterase
-
cross-complementing
- 8-oxo-7,8-dihydroguanine
- fen1
-
unrepaired
-
formamidopyrimidine-dna
-
incises
-
long-patch
-
dna-repair
-
uracil-containing
-
ser326cys
- dihydrouracil
-
arg399gln
- 3'-exonuclease
-
reduction-oxidation
-
enzyme-dna
- medicine
-
gap-filling
-
damage-specific
- analysis
- diagnostics
- biotechnology
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AP 1
-
-
-
-
AP Dnase
-
-
-
-
AP endo
-
-
-
-
AP endonuclease
-
-
-
-
AP endonuclease Class I
-
-
-
-
AP lyase
-
-
-
-
AP-endonuclease
-
-
-
-
Ape
-
-
-
-
APEN
-
-
-
-
APEX nuclease
-
-
-
-
APN1
-
-
-
-
apurinic DNA endonuclease
-
-
-
-
apurinic endodeoxyribonuclease
-
-
-
-
apurinic endonuclease
-
-
-
-
apurinic-apyrimidinic DNA endonuclease
-
-
-
-
apurinic-apyrimidinic endodeoxyribonuclease
-
-
-
-
apurinic-apyrimidinic endonuclease
-
-
-
-
apurinic/apyrimidinic lyase
-
-
-
-
apurinic/apyrimidinic specific endonuclease
-
-
-
-
apyrimidinic endonuclease
-
-
-
-
class II apurinic/apyrimidinic(AP)-endonuclease
-
-
-
-
deoxyribonuclease (apurinic or apyrimidinic)
-
-
-
-
E. coli endonuclease III
-
-
-
-
endodeoxyribonuclease
-
-
-
-
endodeoxyribonuclease III
-
-
-
-
endonuclease III
-
-
-
-
endonuclease VI
-
-
-
-
Escherichia coli endonuclease III
-
-
-
-
HAP1
-
-
-
-
HAP1h
-
-
-
-
Micrococcus luteus UV endonuclease
-
-
-
-
MMH
-
-
-
-
Nfo
-
-
-
-
Ntg1p
-
-
-
-
Ntg2p
-
-
-
-
NTH1
-
-
-
-
nuclease, apurinic endodeoxyribo-
-
-
-
-
nuclease, apurinic-apyrimidinic endodeoxyribo-
-
-
-
-
nuclease, endodeoxyribo-, III
-
-
-
-
phage-T4 UV endonuclease
-
-
-
-
REF-1 protein
-
-
-
-
Ref1
-
-
-
-
UV endo V
-
-
-
-
UV endonuclease
-
-
-
-
UV endonuclease V
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
mechanism
-
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
60184-90-9
-
61811-29-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA
fragments of DNA
-
removes UV light and osmium tetroxide damaged bases via an N-glycosylase activity followed by a 3'-purinic/apyrimidinic endonuclease activity, product is a nucleoside-free site flanked by 3'- and 5'-terminal phosphate groups
-
?
DNA
fragments of DNA
-
incises DNA damaged with UV light, ionizing radiation, OsO4, KMnO4 and H2O2 at cytosine and thymine sites
-
?
DNA
fragments of DNA
-
specific for DNA containing either apurinic or apyrimidinic sites
-
?
additional information
?
-
enzyme plays an important role in repair of DNA damages
-
-
?
additional information
?
-
-
enzyme plays an important role in repair of DNA damages
-
-
?
additional information
?
-
-
important role in repair of oxidative DNA damage
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
enzyme plays an important role in repair of DNA damages
-
-
?
additional information
?
-
-
enzyme plays an important role in repair of DNA damages
-
-
?
additional information
?
-
-
important role in repair of oxidative DNA damage
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
NaCl
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). APEX1_BOVIN
318
0
35570
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
purified APE activity from beef liver mitochondria, determined by SDS-PAGE and Western blot, verified by mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
dialyzed mitochondrial lysates are loaded on a HiTrap Q and SP-Sepharose columns, fractions with APE activity are loaded onto a HiTrap SP column and are further purified using a HiTrap-Heparin column
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Henner, W.D.; Kiker, N.P.; Jorgensen, T.J.; Munck, J.N.
Purification and amino-terminal amino acid sequence of an apurinic/apyrimidinic endonuclease from calf thymus
Nucleic Acids Res.
15
5529-5544
1987
Bos taurus
Doetsch, P.W.; Helland, D.E.; Haseltine, W.A.
Mechanism of action of a mammalian DNA repair endonuclease
Biochemistry
25
2212-2220
1986
Bos taurus
Helland, D.E.; Doetsch, P.W.; Haseltine, W.A.
Substrate specificity of a mammalian DNA repair endonuclease that recognizes oxidative base damage
Mol. Cell. Biol.
6
1983-1990
1986
Bos taurus
Khurshid, R.; Salim, A.; Abbasi, A.
Three-dimensional structure prediction of bovine AP lyase, BAP1: prediction of interaction with DNA and alterations as a result of Arg176-->Ala, Asp282-->Ala, and His308-->Asn mutations
Biochem. Biophys. Res. Commun.
326
711-717
2005
Bos taurus (P23196), Bos taurus
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