4.2.99.B1: DNA 5'-deoxyribose phosphate lyase
This is an abbreviated version!
For detailed information about DNA 5'-deoxyribose phosphate lyase, go to the full flat file.
Word Map on EC 4.2.99.B1
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4.2.99.B1
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glycosylases
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polymerases
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abasic
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neils
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ape1
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8-oxoguanine
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gap-filling
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nei-like
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translesion
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8-oxog
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base-specific
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5-hydroxyuracil
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long-patch
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spiroiminodihydantoin
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y-family
- 4.2.99.B1
- glycosylases
- polymerases
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abasic
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neils
- ape1
- 8-oxoguanine
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gap-filling
-
nei-like
-
translesion
-
8-oxog
-
base-specific
- 5-hydroxyuracil
-
long-patch
- spiroiminodihydantoin
-
y-family
Reaction
catalysis of the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site in DNA where a DNA-(apurinic or apyrimidinic site) lyase has already cleaved the C-O-P bond 3' to the apurinic or apyrimidinic site =
Synonyms
5' dRP lyase, 5'-deoxyribose phosphate lyase, 5'-deoxyribose-5-phosphate lyase, 5'-deoxyribosephosphate lyase, 5'-dRP lyase, 5'-RP lyase, 8-kDa domain dRP lyase, AtPolIA, AtPolIB, beta-pol, beta-pol dRP lyase, deoxyribo-5'-phosphate lyase, DNA beta-polymerase, DNA polymerase beta, DNA polymerase beta deoxyribose phosphate lyase, DNA polymerase gamma, DNA polymerase lambda, DNA polymerase theta, dRP lyase, dRPase, HSV-1 Pol, HSV-1-DNA polymerase, Ku70, Li polbeta, mammalian endonuclease VIII-like protein, NEIL1, NEIL2, pol beta, Pol gamma, pol iota, Pol lambda, Pol theta, PolB, polymerase iota, Rev1, TcPolbeta, TcPolbetaPAK, Trf4, UL30
ECTree
4.2.99.B1 DNA 5'-deoxyribose phosphate lyaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 4.2.99.B1 - DNA 5'-deoxyribose phosphate lyase
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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
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catalysis of the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site in DNA where a DNA-(apurinic or apyrimidinic site) lyase has already cleaved the C-O-P bond 3' to the apurinic or apyrimidinic site. According to the lyase catalytic mechanism, the epsilon-amino group of a catalytic lysine reacts with C1'-carbon of an AP site producing a Schiff base intermediate
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?
additional information
?
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catalysis of the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site in DNA where a DNA-(apurinic or apyrimidinic site) lyase has already cleaved the C-O-P bond 3' to the apurinic or apyrimidinic site. According to the lyase catalytic mechanism, the epsilon-amino group of a catalytic lysine reacts with C1'-carbon of an AP site producing a Schiff base intermediate
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-
?
additional information
?
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catalysis of the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site in DNA where a DNA-(apurinic or apyrimidinic site) lyase has already cleaved the C-O-P bond 3' to the apurinic or apyrimidinic site. According to the lyase catalytic mechanism, the epsilon-amino group of a catalytic lysine reacts with C1'-carbon of an AP site producing a Schiff base intermediate
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?
additional information
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reaction is part of the DNA base excision repair BER
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?
additional information
?
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catalysis of the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site in DNA where a DNA-(apurinic or apyrimidinic site) lyase has already cleaved the C-O-P bond 3' to the apurinic or apyrimidinic site. The reaction mechanism of the lyase reaction involves a transient covalent enzyme-DNA intermediate in the form of a Schiff base connecting Lys72 of the enzyme with the 5'-dRP moiety. The Schiff base intermediate is resolved via a beta-elimination reaction, initiated by abstraction of a C2'-H atom from the 5'-deoxyribose phosphate (5'-dRP) moiety
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?
additional information
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removal of the 5'-deoxyribose phosphate group is a pivotal step in the base excision repair (BER) pathway in vivo
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