4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase
This is an abbreviated version!
For detailed information about DNA-(apurinic or apyrimidinic site) lyase, go to the full flat file.
Word Map on EC 4.2.99.18
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4.2.99.18
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strand
-
exonuclease
-
glycosylases
-
single-stranded
-
pyrimidine
-
endonucleases
-
8-oxoguanine
-
nick
-
thymine
-
uracil
-
duplex
-
genotoxic
-
xrcc1
-
phosphodiester
-
comet
-
deoxyribose
-
methanesulfonate
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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
- 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
Reaction
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
8-oxoG DNA glycosylase, abasic (AP)-endonuclease, abasic endonuclease, AdAPE1/Ref-1, Af0371, Afogg enzyme, ALKBH1, AP 1, AP DNA endonuclease 1, AP Dnase, AP endo, AP endonuclease, AP endonuclease 1, AP endonuclease Ape1, AP endonuclease Class I, AP endonuclease I, AP endonuclease VI, AP lyase, AP site-DNA 5'-phosphomonoester-lyase, AP-endonuclease, AP-endonuclease 1, AP-endonuclease 2, AP-endonuclease/3'-5'exodeoxyribonuclease, AP-lyase, Ap1, Ap2, Ape, APE-1, APE/Ref-1, APE1, APE1/Ref-1, Ape1L, Ape2, APEN, APEX nuclease, APEX1, APLM, APN, APN-1, APN1, apurinic DNA endonuclease, apurinic endodeoxyribonuclease, apurinic endonuclease, apurinic endonuclease 1, apurinic-apyrimidinic DNA endonuclease, apurinic-apyrimidinic endodeoxyribonuclease, apurinic-apyrimidinic endonuclease, apurinic-apyrimidinic endonuclease 1, apurinic-apyrimidinic endonuclease I, apurinic/apyrimidic endonuclease 1, apurinic/Apyrimidinic (AP) endonuclease 1, apurinic/apyrimidinic AP endonuclease, apurinic/apyrimidinic DNA endonuclease 1, apurinic/apyrimidinic endonuclease, apurinic/apyrimidinic endonuclease 1, apurinic/apyrimidinic endonuclease 1/redox factor-1, apurinic/apyrimidinic endonuclease 2, apurinic/apyrimidinic endonuclease APE1, apurinic/apyrimidinic endonuclease-1, apurinic/apyrimidinic endonuclease-1/Redox factor-1, apurinic/apyrimidinic endonuclease/redox effector factor-1, Apurinic/apyrimidinic endonuclease1/redox factor 1, apurinic/apyrimidinic endonuclease1/redox factor-1, apurinic/apyrimidinic lyase, apurinic/apyrimidinic site lyase, apurinic/apyrimidinic specific endonuclease, apurinic/apyrimidinic-endonuclease, apyrimidinic endonuclease, archaeal GO glycosylase, BAP1, class II AP endonuclease LMAP, class II apurinic/apyrimidinic(AP)-endonuclease, class-II AP-endonuclease, deoxyribonuclease (apurinic or apyrimidinic), DNA lyase, DNA polymerase X, DNA-(apurinic or apyrimidinic site) lyase, E. coli endonuclease III, EC 3.1.25.2, EcoNth, Endo III, endodeoxyribonuclease, endodeoxyribonuclease III, EndoIV, endonuclease III, endonuclease IV, endonuclease VI, endonuclease VIII, Escherichia coli endonuclease III, EXO-3, ExoA, ExoA type AP endonuclease, ExoIII, HAP-1, HAP1, HAP1h, hAPE, hAPE1, hNTH, hNTH1, hOgg1 protein, HpXth, human apurinic/apyrimidinic endonuclease, human apurinic/apyrimidinic endonuclease 1, Kae1, KsgA, LplExo, Micrococcus luteus UV endonuclease, MJ0724, mjOgg, MMH, More, mtAPE, MtbXthA, multi-functional apyrimidinic endonuclease1/redox factor-1, N-glycosylase AP lyase, N-glycosylase apurinic/apyrimidinic lyase, NapE, Nei, Nfo, Ntg1, Ntg1p, Ntg2, Ntg2p, Nth, NTH1, nuclease SmnA, nuclease, apurinic endodeoxyribo-, nuclease, apurinic-apyrimidinic endodeoxyribo-, nuclease, endodeoxyribo-, III, Ogg2, oxoG DNA glycosylase, Pa-AGOG, Pa-AGOG DNA glycosylase, PAE2237, PaKae1, PALF, pE296R, PF0258, phage-T4 UV endonuclease, redox effector factor 1, redox factor-1, redox factor-1:Ref-1, Ref-1, REF-1 protein, Ref1, SisExoIII, Smx nuclease, TvoExo, UL30, UV endo V, UV endonuclease, UV endonuclease V, X-ray endonuclease III, XTH, xthA, ZAP1, zApe
ECTree
4.2.99.18 DNA-(apurinic or apyrimidinic site) lyaseAdvanced search results
results (
results (KM Value
KM Value on EC 4.2.99.18 - DNA-(apurinic or apyrimidinic site) lyase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.004
(dA)230*(dT,dU)230
-
ratio dT:dU is 15, partially depyrimidinated by uracil-DNA glycosylase, pH 8
-
0.065
1-amino-4-(4-{(E)-[(4E)-6-chloro-4-[(3-sulfophenyl)imino]-3,4-dihydro-1,3,5-triazin-2(1H)-ylidene]amino}-3-sulfoanilino)-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
-
-
0.000098
12-mer oligodeoxyribonucleotide containing a tetrahydrofuran analogue at the natural AP site
-
wild-type, pH 7.5, 25°C
-
0.000015
30mer THF-T duplex
pH 8.0, 37°C, recombinant His-tagged enzyme
-
0.0000036 - 0.000133
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite G
-
0.0000097 - 0.004
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A
-
0.0000059 - 0.00192
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite G
-
0.00005
DNA containing 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine/C
-
pH 7.5, 37°C
-
0.0000213
DNA containing apurinic/apyrimidinic site
-
pH 7.6, room temperature
-
0.00025
DNA with 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine/C
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pH 7.5, 37°C
0.0000084
duplex oligonucleotide containing a 5,6-dihydro-2'-deoxyuridine*G pair
-
pH 6.8, 37°C, nucleotide incison repair activity
-
0.0000072
duplex oligonucleotide containing a alpha-2'-deoxyadenosine*T pair
-
pH 6.8, 37°C, nucleotide incison repair activity
-
0.0000027
duplex oligonucleotide containing a tetrahydrofuran*G pair
-
pH 6.8, 37°C, nucleotide incison repair activity
-
0.000093
12-mer oligodeoxyribonucleotide containing a natural AP site
-
wild-type, pH 7.5, 25°C
-
0.00022
12-mer oligodeoxyribonucleotide containing a natural AP site
-
mutant Y171F/P173L/N174K, pH 7.5, 25°C
-
0.000048
18-mer containing P33-labeled tetrahydrofuran
-
enzyme dephosphorylated by lambda phosphatase, pH 7.5, 22°C
-
0.000081
18-mer containing P33-labeled tetrahydrofuran
-
enzyme phosphorylated by casein kinase II, pH 7.5, 22°C
-
0.0000091
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite A
-
pH 7.6, 37°C, wild-type enzyme
-
0.14
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite A
-
pH 7.6, 37°C, mutant enzyme R184A
-
0.0000036
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite G
-
pH 7.6, 37°C, wild-type enzyme
-
0.000133
35 base pair oligonucleotide containing 5,6-dihydrouracil opposite G
-
pH 7.6, 37°C, mutant enzyme R184A
-
0.0000097
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A
-
pH 7.6, 37°C, wild-type enzyme
-
0.004
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A
-
pH 7.6, 37°C, mutant enzyme R184A
-
0.0000059
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite G
-
pH 7.6, 37°C, wild-type enzyme
-
0.00192
35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite G
-
pH 7.6, 37°C, mutant enzyme R184A
-
0.0000034
43-mer oligonucleotide containing apurinic/apyrimidinic sites
37°C, wild-type enzyme
-
0.0000136
43-mer oligonucleotide containing apurinic/apyrimidinic sites
37°C, mutant enzyme N226A
-
0.0000184
43-mer oligonucleotide containing apurinic/apyrimidinic sites
37°C, mutant enzyme N229A
-
0.0000278
43-mer oligonucleotide containing apurinic/apyrimidinic sites
37°C, mutant enzyme N226A/N229A
-
0.0000368
43-mer oligonucleotide containing the AP-site analog THF at nt 31
-
wild-type, presence of 2 mM Mg2+
-
0.0000536
43-mer oligonucleotide containing the AP-site analog THF at nt 31
-
mutant C99S, presence of 2 mM Mg2+
-
0.0000035
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite T
0.0000066
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite C
0.0000085
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite G
0.000038
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite A
0.000042
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite G
0.000054
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant deltaQLY, Nei placed opposite G
0.000077
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite G
0.00014
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite C
0.00016
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant QLY/AAA, Nei placed opposite T
0.00016
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite A
0.00026
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite A
0.00027
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite C
0.0014
5'-CTCTCCCTTC-5,6-dihydrouracil-CTCCTTTCCTCT-3'
mutant Q261A, Nei placed opposite T
0.00058
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite G
0.00061
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite A
0.00068
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite C
0.0013
5'-CTCTCCCTTC-8-oxo-7,8-dihydroguanine-CTCCTTTCCTCT-3'
wild-type, Nei placed opposite T
0.0000642
5'-Cy3-CAAGGTAGTrUATCCTTG-1-Black Hole Quencher1-3'
-
native enzyme
-
0.000424
5'-Cy3-CAAGGTAGTrUATCCTTG-1-Black Hole Quencher1-3'
-
recombinant enzyme
-
0.0000023
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite G
0.0000032
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite A
0.0000044
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite C
0.0000044
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite T
0.000049
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant QLY/AAA, Nei placed opposite G
0.000066
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant deltaQLY, Nei placed opposite A
0.00019
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant QLY/AAA, Nei placed opposite T
0.00024
5'-GACAAGCGCAG-(5R,6S)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant Q261A, Nei placed opposite G
0.0000023
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite G
0.0000046
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite T
0.0000047
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite C
0.000016
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
wild-type, Nei placed opposite A
0.00021
5'-GACAAGCGCAG-(5S,6R)-2'-deoxy-5,6-dihydroxyuridine-CAGCCGAACAC-3'
mutant Q261A, Nei placed opposite G
0.00082
5'-TCGAGGATCCTGAGCTCGAGTCGACGXTCGCGAATTCTGCGGATCCAAGC-3'
pH 7.5, 37°C
-
0.00091
5'-TCGAGGATCCTGAGCTCGAGTCGACGXTCGCGAATTCTGCGGATCCAAGC-3'
pH 7.5, 37°C
-
0.000088
AP-DNA
-
wild-type in rAP-containing oligonucleotide cleavage assay
-
0.00012
AP-DNA
-
mutant Y72F in rAP-containing oligonucleotide cleavage assay
-
0.0075
AP-DNA
-
mutant Y72A in rAP-containing oligonucleotide cleavage assay
-
0.011
AP-DNA
-
mutant R37A in rAP-containing oligonucleotide cleavage assay
-
0.000026
DNA containing 5-hydroxy-2'-deoxyuridine/G
-
pH 7.5, 37°C
-
0.00000007
DNA containing 5-OH-C/A
-
wild-type, pH 7.5, 37°C, presence of EDTA
-
0.00000014
DNA containing 5-OH-C/A
-
P211R mutant, pH 7.5, 37°C, presence of Mg2+
-
0.0000002
DNA containing 5-OH-C/A
-
P211R mutant, pH 7.5, 37°C, presence of EDTA
-
0.0000017
DNA containing 5-OH-C/A
-
G212 mutant, pH 7.5, 37°C, presence of Mg2+
-
0.0000035
DNA containing 5-OH-C/A
-
G212 mutant, pH 7.5, 37°C, presence of EDTA
-
0.000000048
DNA containing 5-OH-C/G
-
P211R mutant, pH 7.5, 37°C, presence of Mg2+
-
0.00000005
DNA containing 5-OH-C/G
-
wild-type, pH 7.5, 37°C, presence of Mg2+ or EDTA
-
0.00000009
DNA containing 5-OH-C/G
-
P211R mutant, pH 7.5, 37°C, presence of EDTA
-
0.000001
DNA containing 5-OH-C/G
-
G212 mutant, pH 7.5, 37°C, presence of EDTA
-
0.0000012
DNA containing 5-OH-C/G
-
G212 mutant, pH 7.5, 37°C, presence of Mg2+
-
100
DNA containing an abasic site
-
pH 7.5, wild-type enzyme, low salt concentration (82 mM NaCl)
108
DNA containing an abasic site
-
pH 7.5, mutant enzyme Y128A, high salt concentration (150 mM NaCl)
110
DNA containing an abasic site
-
pH 7.5, wild-type enzyme, high salt concentration (150 mM NaCl)
140
DNA containing an abasic site
-
pH 7.5, mutant enzyme Y128A, low salt concentration (82 mM NaCl)
165
DNA containing an abasic site
-
pH 7.5, mutant enzyme Y269A, low salt concentration (82 mM NaCl)
255
DNA containing an abasic site
-
pH 7.5, mutant enzyme Y171F, low salt concentration (82 mM NaCl)
310
DNA containing an abasic site
-
pH 7.5, mutant enzyme Y171A, high salt concentration (150 mM NaCl)
360
DNA containing an abasic site
-
pH 7.5, mutant enzyme Y171A, low salt concentration (82 mM NaCl)
413
DNA containing an abasic site
-
pH 7.5, mutant enzyme Y269A, high salt concentration (150 mM NaCl)
0.000000083
DNA containing apurinic/apyrimidinic sites
wild-type, Nei placed opposite A
-
0.00000011
DNA containing apurinic/apyrimidinic sites
wild-type, Nei placed opposite G
-
0.000022
DNA containing apurinic/apyrimidinic sites
mutant QLY/AAA, Nei placed opposite G
-
0.000028
DNA containing apurinic/apyrimidinic sites
mutant QLY/AAA, Nei placed opposite A
-
0.000136
THF-containing oligonucleotide
-
APE1 mutant D70A, AP endonuclease activity
-
0.000184
THF-containing oligonucleotide
-
LMAP mutant A138D, AP endonuclease activity
-
additional information
AP-DNA
-
not detected in mutant E261Q in rAP-containing oligonucleotide cleavage assay
-
additional information
additional information
steady-state kinetic analysis
-
additional information
additional information
-
steady-state kinetic analysis
-
additional information
additional information
-
Km for AP cleavage is similar to that for 5'-deoxyribose-5-phosphate removal, it explains the relative difference in apurinic/apyrimidinic cleavage observed with the plasmid and apurinic/apyrimidinic duplex oligonucleotide with the former containing a 100fold higher concentration of apurinic/apyrimidinic sites (100 uracil residues per plasmid molecule) than the oligonucleotides-based substrate.
-
additional information
additional information
-
Steady-state kinetic analysis of Ape1 AP endonuclease activity at 10 mM Mg2+ with and without 5 mM ATP indicates a less than 2fold difference in KM-value but an 19fold enhancement in kcat in the presence of ATP, suggesting an enhancement of the catalytic reaction specifically
-
additional information
additional information
kinetic analysis of human 8-oxoguanine-DNA glycosylase activation through APE1, overview
-
additional information
additional information
-
kinetic analysis of human 8-oxoguanine-DNA glycosylase activation through APE1, overview
-
additional information
additional information
kinetic mechanism of 3'-end nucleotide removal in the 3'-5'-exonuclease process catalyzed by APE1 under pre-steady-state conditions, interaction of enzyme APE1 with DNA containing an abasic site, overview
-
additional information
additional information
-
kinetic mechanism of 3'-end nucleotide removal in the 3'-5'-exonuclease process catalyzed by APE1 under pre-steady-state conditions, interaction of enzyme APE1 with DNA containing an abasic site, overview
-
additional information
additional information
measurement of conformational dynamics of DNA at pre-steady-state conditions, stopped-flow measurements. Rate and equilibrium constants for wild-type enzyme and mutant H83A Apn1 interactions with DNA substrates F(2-aPu) and AP(2-aPu), F is tetrahydrofuran
-
additional information
additional information
-
measurement of conformational dynamics of DNA at pre-steady-state conditions, stopped-flow measurements. Rate and equilibrium constants for wild-type enzyme and mutant H83A Apn1 interactions with DNA substrates F(2-aPu) and AP(2-aPu), F is tetrahydrofuran
-
additional information
additional information
Michaelis-Menten kinetic study, overview
-
additional information
additional information
-
Michaelis-Menten kinetic study, overview
-
additional information
additional information
pre-steady-state kinetic analysis of structural rearrangements of the DNA substrates and uncleavable ligands during their interaction with Endo III
-
additional information
additional information
-
pre-steady-state kinetic analysis of structural rearrangements of the DNA substrates and uncleavable ligands during their interaction with Endo III
-
additional information
additional information
pre-steady-state kinetic analysis, kinetic analysis of DNA binding, stopped flow measurements, overview
-
additional information
additional information
-
pre-steady-state kinetic analysis, kinetic analysis of DNA binding, stopped flow measurements, overview
-
additional information
additional information
rate constants of DNA substrate cleavage by APE1 and dissociation constants of APE1/DNA substrate complexes. Analysis of efficacy of APE1 binding to modified DNA duplexes and kinetics of enzyme-substrate complex formation by stopped flow measurements, kinetics, overview
-
additional information
additional information
-
rate constants of DNA substrate cleavage by APE1 and dissociation constants of APE1/DNA substrate complexes. Analysis of efficacy of APE1 binding to modified DNA duplexes and kinetics of enzyme-substrate complex formation by stopped flow measurements, kinetics, overview
-
additional information
additional information
stopped-flow fluorescence measurements, kinetic analysis of nucleotide incision repair (NIR) pathway compared to base excision DNA repair (BER) pathway. Rate constants of wild-type Apn1 interaction with substrate DHU(2-aPu), overview. Proposed kinetic mechanisms, containing two or three binding steps, for the interaction of wild-type Apn1 with substrate DHU(2-aPu)
-
additional information
additional information
stopped-flow fluorescence techniques to conduct a comparative kinetic analysis of the conformational transitions in human apurinic/apyrimidinic endonuclease 1 (APE1) and in DNA containing an abasic site in the course of their interaction. Influence of different concentrations of Mg2+ and other metal ions on stopped-flow kinetics, overview
-
additional information
additional information
-
stopped-flow fluorescence techniques to conduct a comparative kinetic analysis of the conformational transitions in human apurinic/apyrimidinic endonuclease 1 (APE1) and in DNA containing an abasic site in the course of their interaction. Influence of different concentrations of Mg2+ and other metal ions on stopped-flow kinetics, overview
-
additional information
additional information
steady-state Michaelis-Menten kinetic analysis
-
additional information
additional information
-
steady-state Michaelis-Menten kinetic analysis
-
