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2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
-
in ssDNA
-
-
?
5'-AAAGAGAAAGAGAAACCCAAAGAGGAAAGGTGAGGAGAA-3' + H2O
5'-AAAGAGAAAGAGAAACCUAAAGAGGAAAGGTGAGGAGAA-3' + NH3
-
the enzyme targets 5'-CCCA-3' sequences with 5'-AAACCCAAA-3' recognized most efficiently
-
-
?
5'-ATTCCCAATT-3' + H2O
5'-ATTCCUAATT-3'
-
-
-
?
5-methylcytosine in single-stranded DNA + H2O
?
the enzyme exhibits low activity toward 5-methylcytosine n single-stranded DNA
-
-
?
cytidine in HIV-1 virus ssDNA + H2O
uridine in HIV-1 virus ssDNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
deoxycytosine in single-stranded viral DNA + H2O
deoxyuridine in single-stranded viral DNA + NH3
-
-
-
?
TTTCCCCGC + H2O
TTTCCUCGC + NH3
sequence with highest deamination rate
-
-
?
additional information
?
-
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
-
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the APOBEC3 enzymes are a double-edged sword that can catalyze deamination of cytosine in genomic DNA, which results in potential genomic instability due to the many mutagenic fates of uracil. The enzymes must be able to efficiently deaminate transiently available single-stranded DNA during reverse transcription, replication, or transcription. Specific biochemical characteristics promote deamination in each situation to increase enzyme efficiency through processivity, rapid enzyme cycling between substrates, or oligomerization state
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme restricts the infectivity of viruses, such as HIV-1, by targeting CCC hotspots scattered through minus DNA strands, reverse-transcribed from genomic RNA
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
relatively low deaminase activity and selectivity for methylated cytosine
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme preferentially converts cytidine to uridine at the third position of triplet cytosine (CCC) hotspots. The phosphate backbone is required for C-terminal domain of the enzyme to slide along the DNA strand and to exert the 3'->5' polarity. The higher the salt cncentration, the less prominent is the 3'->5' polarity
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
-
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
-
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
cytosine deamination occurs preferentially in CpC (5'GpG/CpC5')
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
in vitro, the enzyme has a preferred sequence motif of T/CCC and shows a 3'->5' like processivity
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
native enzyme demonstrates a preference for deamination of the C residue proximal to the 5'-ssDNA end in the 5'CCC motif and deaminates the two C residues processively
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
phage M13mp2 circular DNA containing a series of in-frame 5'-AAACCCAAA hot motifs embedded in lacZalpha reporter sequence located within a single-stranded gapped region of M13 double-stranded DNA. The third C in the 5'-AAACCCAAA motif is deaminated predominantly
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
the enzyme carries out processive cytosine deamination by randomly binding, sliding and jumping bidirectionally on single-stranded DNA. The deamination by the enzyme proceeds predominantly 3'->5', resulting in preferential deamination at the target located closer to the 5' end of substrate. The enzyme favors deamination at the 5'C residue in the hot-spot motif CCC
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
the enzyme strongly prefers cytosines in a run of C's usually targeting the last base in the run. The enzyme readily converts the third cytosine in CCC to uracil but does not convert the first or the second cytosine in the sequence at detectable levels
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
the enzyme targets 5'-CCCA-3' sequences with 5'-AAACCCAAA-3' recognized most efficiently
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
the full-length enzyme processively deaminates cytidine in two 5'-CCC-3' motifs located on a single-stranded DNA substrate, during one binding event. The full-length enzyme also exerts a 3' to 5' deamination bias by preferentially deaminating the cytidine in the CCC motif near the 5'end of the single-stranded DNA substrate
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
minus strand deamination occurs preferentially at a CCCA sequence. The third cytidine of the d(CCCA) segment is deaminated at an early stage and that then the second one is deaminated at a late stage, so the deamination is carried out in a strict 3'-5' order
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
the APOBEC3 enzymes are a double-edged sword that can catalyze deamination of cytosine in genomic DNA, which results in potential genomic instability due to the many mutagenic fates of uracil. The enzymes must be able to efficiently deaminate transiently available single-stranded DNA during reverse transcription, replication, or transcription. Specific biochemical characteristics promote deamination in each situation to increase enzyme efficiency through processivity, rapid enzyme cycling between substrates, or oligomerization state
-
-
?
additional information
?
-
-
APOBEC3G cytidine deaminase contracts ssDNA in a deamination motif-dependent manner, presence of bidirectional quasi-localized scanning of APOBEC3G cytidine deaminase occurring proximal to a 5' hot motif, a motif-dependent DNA contraction greatest for 5' hot before 3' hot before 5' cold motifs, and diminished mobility at low salt, overview
-
-
?
additional information
?
-
-
the preferred sequence context for wild-type hA3G is GG. In the CD2-1 mutant variants, both TGG and GGG are preferred, while the wild-type prefers TGG
-
-
?
additional information
?
-
-
the enzyme binds randomly to single-stranded DNA, then jumps and slides processively to deaminate target motifs. Preferential deamination of the third C is observed in the motif 5'-AAACCCAAA-3' while deamination at the first C is not observed. The replacement of AAA with TTT at the 3' side of CCC results in a 20fold inhibition of deamination. The replacement of AGA by TTT at the 5' side of CCC results in about a 5fold reduction in specific activity. Similar binding constants are observed with single-stranded DNA substrates ranging from 10 to 69 nucleotides whereas binding is reduced sharply for a 9-nucleotide substrate. When confronting partially double-stranded DNA, to which the enzyme cannot bind, sliding is lost but jumping is retained. The enzyme shows catalytic orientational specificity such that deamination occurs predominantly 3'-5' without requiring hydrolysis of a nucleotide cofactor
-
-
?
additional information
?
-
the enzyme binds with similar efficiency to the 5' and 3' single-stranded DNA substrates and binds the single-stranded region of the gap-DNA substrates with the same efficiency as tail-DNA. Enzyme monomers, dimers, and higher-order oligomers can bind single-stranded DNA substrates in a manner independent of strand polarity and availability of free single-stranded DNA ends. The efficiency of complex formation decreases about 3 times for the 18single-stranded-tail-DNA compared to that for the longer 69single-stranded-tail-DNA hybrid substrate
-
-
?
additional information
?
-
the enzyme deaminates C -> U on single-stranded DNA, but favors 5'CCCC target motifs with a preference for the 3'C, and its specific activity is strongly influenced by nucleotides surrounding the 5'CCC target motif
-
-
?
additional information
?
-
-
the enzyme deaminates C -> U on single-stranded DNA, but favors 5'CCCC target motifs with a preference for the 3'C, and its specific activity is strongly influenced by nucleotides surrounding the 5'CCC target motif
-
-
?
additional information
?
-
-
the enzyme does not effectively bind substrates shorter than 10 nucleotides. Substrates containing 5'-methyldeoxycytidine 2'-deoxy-5-aza-5,6-dihydrocytidine, 2'-deoxy-4-ethylcytidine and 2'-deoxyzebularine at position -1 are deaminated by the enzyme with 62%, 25%, 19%, and 9% efficiency, respectively, Substrates containing N3-methyl cytidine or isocytidine at position -1 are not appreciably deaminated by the enzyme
-
-
?
additional information
?
-
-
the enzyme has a catalytically inactive N-terminal CD1 domain that mediates processivity and an active C-terminal CD2 domain that catalyzes deaminations. The enzyme cannot bind well to double-stranded DNA. Native enzyme is still able to processively deaminate two C residues with a double-stranded DNA region in-between, but with a 2fold decrease in the processivity factor
-
-
?
additional information
?
-
the enzyme alone extensively deaminates cDNA independently of reverse transcriptase. The cDNA has to be free of its RNA template to allow deamination. Deoxycytosine or dCTP are poor substrates
-
-
?
additional information
?
-
the enzyme cannot readily deaminate a cytosine dinucleotide in single-stranded DNA stem structures or in nucleotide base loops composed of three bases. Single-stranded nucleotide loops up to seven bases in length are poor targets for enzyme activity unless cytosine residues flank the cytosine dinucleotide. The enzyme favors adenines, cytosines and thymines flanking the cytosine dinucleotide target in unstructured regions of single-stranded DNA. Low cytosine deaminase activity is detected when guanines flank the cytosine dinucleotide
-
-
?
additional information
?
-
intrinsic DNA cytidine deaminase activity of full-length A3G is measured by expressing these proteins in ung-deficient Escherichia coli BW310 and by quantifying the frequency of RifR-conferring rpoB mutations
-
-
?
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2'-deoxycytidine + H2O
2'-deoxyuridine + NH3
-
in ssDNA
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
deoxycytosine in single-stranded viral DNA + H2O
deoxyuridine in single-stranded viral DNA + NH3
-
-
-
?
additional information
?
-
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the APOBEC3 enzymes are a double-edged sword that can catalyze deamination of cytosine in genomic DNA, which results in potential genomic instability due to the many mutagenic fates of uracil. The enzymes must be able to efficiently deaminate transiently available single-stranded DNA during reverse transcription, replication, or transcription. Specific biochemical characteristics promote deamination in each situation to increase enzyme efficiency through processivity, rapid enzyme cycling between substrates, or oligomerization state
-
-
?
cytosine in single-stranded DNA + H2O
uracil in single-stranded DNA + NH3
the enzyme restricts the infectivity of viruses, such as HIV-1, by targeting CCC hotspots scattered through minus DNA strands, reverse-transcribed from genomic RNA
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
-
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
-
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
cytosine deamination occurs preferentially in CpC (5'GpG/CpC5')
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
in vitro, the enzyme has a preferred sequence motif of T/CCC and shows a 3'->5' like processivity
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
native enzyme demonstrates a preference for deamination of the C residue proximal to the 5'-ssDNA end in the 5'CCC motif and deaminates the two C residues processively
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
phage M13mp2 circular DNA containing a series of in-frame 5'-AAACCCAAA hot motifs embedded in lacZalpha reporter sequence located within a single-stranded gapped region of M13 double-stranded DNA. The third C in the 5'-AAACCCAAA motif is deaminated predominantly
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
the enzyme carries out processive cytosine deamination by randomly binding, sliding and jumping bidirectionally on single-stranded DNA. The deamination by the enzyme proceeds predominantly 3'->5', resulting in preferential deamination at the target located closer to the 5' end of substrate. The enzyme favors deamination at the 5'C residue in the hot-spot motif CCC
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
the enzyme strongly prefers cytosines in a run of C's usually targeting the last base in the run. The enzyme readily converts the third cytosine in CCC to uracil but does not convert the first or the second cytosine in the sequence at detectable levels
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
-
the enzyme targets 5'-CCCA-3' sequences with 5'-AAACCCAAA-3' recognized most efficiently
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
the full-length enzyme processively deaminates cytidine in two 5'-CCC-3' motifs located on a single-stranded DNA substrate, during one binding event. The full-length enzyme also exerts a 3' to 5' deamination bias by preferentially deaminating the cytidine in the CCC motif near the 5'end of the single-stranded DNA substrate
-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
the APOBEC3 enzymes are a double-edged sword that can catalyze deamination of cytosine in genomic DNA, which results in potential genomic instability due to the many mutagenic fates of uracil. The enzymes must be able to efficiently deaminate transiently available single-stranded DNA during reverse transcription, replication, or transcription. Specific biochemical characteristics promote deamination in each situation to increase enzyme efficiency through processivity, rapid enzyme cycling between substrates, or oligomerization state
-
-
?
additional information
?
-
-
the enzyme binds randomly to single-stranded DNA, then jumps and slides processively to deaminate target motifs. Preferential deamination of the third C is observed in the motif 5'-AAACCCAAA-3' while deamination at the first C is not observed. The replacement of AAA with TTT at the 3' side of CCC results in a 20fold inhibition of deamination. The replacement of AGA by TTT at the 5' side of CCC results in about a 5fold reduction in specific activity. Similar binding constants are observed with single-stranded DNA substrates ranging from 10 to 69 nucleotides whereas binding is reduced sharply for a 9-nucleotide substrate. When confronting partially double-stranded DNA, to which the enzyme cannot bind, sliding is lost but jumping is retained. The enzyme shows catalytic orientational specificity such that deamination occurs predominantly 3'-5' without requiring hydrolysis of a nucleotide cofactor
-
-
?
additional information
?
-
the enzyme binds with similar efficiency to the 5' and 3' single-stranded DNA substrates and binds the single-stranded region of the gap-DNA substrates with the same efficiency as tail-DNA. Enzyme monomers, dimers, and higher-order oligomers can bind single-stranded DNA substrates in a manner independent of strand polarity and availability of free single-stranded DNA ends. The efficiency of complex formation decreases about 3 times for the 18single-stranded-tail-DNA compared to that for the longer 69single-stranded-tail-DNA hybrid substrate
-
-
?
additional information
?
-
the enzyme deaminates C -> U on single-stranded DNA, but favors 5'CCCC target motifs with a preference for the 3'C, and its specific activity is strongly influenced by nucleotides surrounding the 5'CCC target motif
-
-
?
additional information
?
-
-
the enzyme deaminates C -> U on single-stranded DNA, but favors 5'CCCC target motifs with a preference for the 3'C, and its specific activity is strongly influenced by nucleotides surrounding the 5'CCC target motif
-
-
?
additional information
?
-
-
the enzyme does not effectively bind substrates shorter than 10 nucleotides. Substrates containing 5'-methyldeoxycytidine 2'-deoxy-5-aza-5,6-dihydrocytidine, 2'-deoxy-4-ethylcytidine and 2'-deoxyzebularine at position -1 are deaminated by the enzyme with 62%, 25%, 19%, and 9% efficiency, respectively, Substrates containing N3-methyl cytidine or isocytidine at position -1 are not appreciably deaminated by the enzyme
-
-
?
additional information
?
-
-
the enzyme has a catalytically inactive N-terminal CD1 domain that mediates processivity and an active C-terminal CD2 domain that catalyzes deaminations. The enzyme cannot bind well to double-stranded DNA. Native enzyme is still able to processively deaminate two C residues with a double-stranded DNA region in-between, but with a 2fold decrease in the processivity factor
-
-
?
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(12bS)-5,6,6a,7,8,12b-hexahydrobenzo[a]phenanthridine-10,11-diol
-
(1R,2S)-2-(methylamino)-1-phenylpropan-1-ol
-
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoic acid
-
(2S)-3-(3,4-dihydroxyphenyl)-2-hydrazinyl-2-methylpropanoic acid
-
(3,4-dihydroxyphenyl)acetic acid
-
(5E)-N-methyl-2,3-diphenyl-1,2,4-thiadiazol-5(2H)-imine
-
(6aR)-6-(prop-2-en-1-yl)-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
-
(6aR)-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
-
(6aR)-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-2,10,11-triol
-
(6aR)-6-propyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
-
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[2-[(pyridin-4-yl)sulfanyl]acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
1-phenyl-2,3,4,5-tetrahydro-1H-3-benzazepine-7,8-diol
-
2-amino-3-(2,4,5-trihydroxyphenyl)propanoic acid
-
2-phenyl-1,2-benzoselenazol-3(2H)-one
-
2-[(E)-2-(3,4-dihydroxyphenyl)ethenyl]-6-hydroxy-4H-pyran-4-one
-
2-[methyl(nitroso)amino]benzene-1,4-diol
-
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-yl)methanediyl]bis(6-hydroxybenzoic acid)
-
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one
-
4,4'-(2,3-dimethylbutane-1,4-diyl)dibenzene-1,2-diol
-
4-(4,5,6,7-tetrahydrothieno[2,3-c]pyridin-4-yl)benzene-1,2-diol
-
4-amino-5-methyl-1,2,4-triazole-3-thiol
-
-
4-[(2-sulfanyl-1H-imidazol-1-yl)methyl]phenol
-
4-[(4-bromobenzylidene)amino]-1,2,4-triazole-3-thiol
-
MN256.0105, 99% inhibition at 0.02 mM
4-[(4-methoxybenzylidene)amino]-5-methyl-1,2,4-triazole-3-thiol
-
-
4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]benzene-1,2-diol
-
4-[methyl(nitroso)amino]benzene-1,2-diol
-
6-amino-5,6,7,8-tetrahydronaphthalene-2,3-diol
-
aurothio-beta-D-glucose
-
cyclohexa-2,5-diene-1,4-dione
-
methyl 2-amino-3-(3,4-dihydroxyphenyl)propanoate
-
N-(3-thio-5-methyl-1,2,4-triazol-4-yl)benzamide
-
-
N-[(4bS,8R,8aS)-7-(cyclopropylmethyl)-1,8a-dihydroxy-5,6,7,8,8a,9,14,14b-octahydro-4,8-methano[1]benzofuro[2,3-a]pyrido[4,3-b]carbazol-11-yl]guanidine
-
N-[2-(3,4-dihydroxyphenyl)ethyl]acetamide
-
p-chloromercuribenzoate
-
tetrasodium 3-[(E)-[4-formyl-5,6-dihydroxy-3-[(phosphonatoperoxy)methyl]pyridin-2-yl]diazenyl]-7-nitronaphthalene-1,5-disulfonate
-
additional information
-
not inhibited by 4-amino-1,2,4-triazol-3-ol, 4-amino-5-methyl-1,2,4-triazol-3-ol, 6-(4-methoxyphenyl)-3-methyl-1,2,4-triazolo[3,4-b]-[1,3,4]thiadiazole, and 3-(benzylthio)-5-methyl-1,2,4-triazol-4-amine
-
additional information
the virion infectivity factor of HIV binds cytoplasmic enzyme marking it for degradation
-
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0.00819 - 0.3944
5'-ATTCCCAATT-3'
0.0119 - 0.395
cytidine in HIV-1 virus ssDNA
-
0.01615 - 0.3944
cytosine in single-stranded viral DNA
-
additional information
additional information
-
pre-steady state and steady state kinetics, stopped-flow fluorescence measurements, detailed overview
-
0.00819
5'-ATTCCCAATT-3'
mutant P210A, pH 7.5, 20°C
0.0119
5'-ATTCCCAATT-3'
mutant D370A, pH 7.5, 20°C
0.0162
5'-ATTCCCAATT-3'
mutant Q380A, pH 7.5, 20°C
0.0185
5'-ATTCCCAATT-3'
mutant P210G, pH 7.5, 20°C
0.0204
5'-ATTCCCAATT-3'
wild-type, pH 7.5, 20°C
0.0225
5'-ATTCCCAATT-3'
mutant F268A, pH 7.5, 20°C
0.0331
5'-ATTCCCAATT-3'
mutant H248G, pH 7.5, 20°C
0.0333
5'-ATTCCCAATT-3'
mutant H250A, pH 7.5, 20°C
0.0632
5'-ATTCCCAATT-3'
mutant R376A, pH 7.5, 20°C
0.1639
5'-ATTCCCAATT-3'
mutant R256A, pH 7.5, 20°C
0.271
5'-ATTCCCAATT-3'
mutant R374A, pH 7.5, 20°C
0.2785
5'-ATTCCCAATT-3'
mutant Q245A, pH 7.5, 20°C
0.3944
5'-ATTCCCAATT-3'
mutant D264A, pH 7.5, 20°C
0.0119
cytidine in HIV-1 virus ssDNA
mutant D370A, pH not specified in the publication, temperature not specified in the publication
-
0.0162
cytidine in HIV-1 virus ssDNA
mutant Q380A, pH not specified in the publication, temperature not specified in the publication
-
0.0185
cytidine in HIV-1 virus ssDNA
mutant P210G, pH not specified in the publication, temperature not specified in the publication
-
0.0204
cytidine in HIV-1 virus ssDNA
wild-type, pH not specified in the publication, temperature not specified in the publication
-
0.0225
cytidine in HIV-1 virus ssDNA
mutant F268A, pH not specified in the publication, temperature not specified in the publication
-
0.0271
cytidine in HIV-1 virus ssDNA
mutant R374A, pH not specified in the publication, temperature not specified in the publication
-
0.0331
cytidine in HIV-1 virus ssDNA
mutant H248G, pH not specified in the publication, temperature not specified in the publication
-
0.0333
cytidine in HIV-1 virus ssDNA
mutant H250A, pH not specified in the publication, temperature not specified in the publication
-
0.0632
cytidine in HIV-1 virus ssDNA
mutant R376A, pH not specified in the publication, temperature not specified in the publication
-
0.0819
cytidine in HIV-1 virus ssDNA
mutant P210A, pH not specified in the publication, temperature not specified in the publication
-
0.164
cytidine in HIV-1 virus ssDNA
mutant R256A, pH not specified in the publication, temperature not specified in the publication
-
0.279
cytidine in HIV-1 virus ssDNA
mutant Q245A, pH not specified in the publication, temperature not specified in the publication
-
0.395
cytidine in HIV-1 virus ssDNA
mutant D264A, pH not specified in the publication, temperature not specified in the publication
-
0.01615
cytosine in single-stranded viral DNA
mutant enzyme Q380A, at pH 7.5 and 37°C
-
0.01846
cytosine in single-stranded viral DNA
mutant enzyme P210G, at pH 7.5 and 37°C
-
0.02042
cytosine in single-stranded viral DNA
wild type enzyme, at pH 7.5 and 37°C
-
0.02252
cytosine in single-stranded viral DNA
mutant enzyme F268A, at pH 7.5 and 37°C
-
0.02705
cytosine in single-stranded viral DNA
mutant enzyme R374A, at pH 7.5 and 37°C
-
0.03306
cytosine in single-stranded viral DNA
mutant enzyme H248G, at pH 7.5 and 37°C
-
0.03325
cytosine in single-stranded viral DNA
mutant enzyme H250A, at pH 7.5 and 37°C
-
0.06323
cytosine in single-stranded viral DNA
mutant enzyme R376A, at pH 7.5 and 37°C
-
0.08188
cytosine in single-stranded viral DNA
mutant enzyme P210A, at pH 7.5 and 37°C
-
0.1189
cytosine in single-stranded viral DNA
mutant enzyme D370A, at pH 7.5 and 37°C
-
0.1639
cytosine in single-stranded viral DNA
mutant enzyme R256A, at pH 7.5 and 37°C
-
0.2785
cytosine in single-stranded viral DNA
mutant enzyme Q245A, at pH 7.5 and 37°C
-
0.3944
cytosine in single-stranded viral DNA
mutant enzyme D264A, at pH 7.5 and 37°C
-
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0.0001 - 0.014
5'-ATTCCCAATT-3'
0.0001 - 0.008
cytidine in HIV-1 virus ssDNA
-
0.000083 - 0.008
cytosine in single-stranded viral DNA
-
0.0001
5'-ATTCCCAATT-3'
mutant P210A, pH 7.5, 20°C
0.0001
5'-ATTCCCAATT-3'
mutant R374A, pH 7.5, 20°C
0.0002
5'-ATTCCCAATT-3'
mutant D370A, pH 7.5, 20°C
0.0002
5'-ATTCCCAATT-3'
mutant P210G, pH 7.5, 20°C
0.0002
5'-ATTCCCAATT-3'
mutant R256A, pH 7.5, 20°C
0.0005
5'-ATTCCCAATT-3'
mutant F268A, pH 7.5, 20°C
0.0009
5'-ATTCCCAATT-3'
mutant R376A, pH 7.5, 20°C
0.001
5'-ATTCCCAATT-3'
mutant Q380A, pH 7.5, 20°C
0.0018
5'-ATTCCCAATT-3'
wild-type, pH 7.5, 20°C
0.0018
5'-ATTCCCAATT-3'
mutant D264A, pH 7.5, 20°C
0.0047
5'-ATTCCCAATT-3'
mutant H248G, pH 7.5, 20°C
0.008
5'-ATTCCCAATT-3'
mutant H250A, pH 7.5, 20°C
0.014
5'-ATTCCCAATT-3'
mutant Q245A, pH 7.5, 20°C
0.0001
cytidine in HIV-1 virus ssDNA
mutant P210A, pH not specified in the publication, temperature not specified in the publication
-
0.0001
cytidine in HIV-1 virus ssDNA
mutant R374A, pH not specified in the publication, temperature not specified in the publication
-
0.0002
cytidine in HIV-1 virus ssDNA
mutant D370A, pH not specified in the publication, temperature not specified in the publication
-
0.0002
cytidine in HIV-1 virus ssDNA
mutant P210G, pH not specified in the publication, temperature not specified in the publication
-
0.0005
cytidine in HIV-1 virus ssDNA
mutant F268A, pH not specified in the publication, temperature not specified in the publication
-
0.0009
cytidine in HIV-1 virus ssDNA
mutant R376A, pH not specified in the publication, temperature not specified in the publication
-
0.001
cytidine in HIV-1 virus ssDNA
mutant Q380A, pH not specified in the publication, temperature not specified in the publication
-
0.0014
cytidine in HIV-1 virus ssDNA
mutant Q245A, pH not specified in the publication, temperature not specified in the publication
-
0.0018
cytidine in HIV-1 virus ssDNA
wild-type, pH not specified in the publication, temperature not specified in the publication
-
0.0018
cytidine in HIV-1 virus ssDNA
mutant D264A, pH not specified in the publication, temperature not specified in the publication
-
0.002
cytidine in HIV-1 virus ssDNA
mutant R256A, pH not specified in the publication, temperature not specified in the publication
-
0.0047
cytidine in HIV-1 virus ssDNA
mutant H248G, pH not specified in the publication, temperature not specified in the publication
-
0.008
cytidine in HIV-1 virus ssDNA
mutant H250A, pH not specified in the publication, temperature not specified in the publication
-
0.000083
cytosine in single-stranded viral DNA
mutant enzyme R374A, at pH 7.5 and 37°C
-
0.000102
cytosine in single-stranded viral DNA
mutant enzyme P210A, at pH 7.5 and 37°C
-
0.000165
cytosine in single-stranded viral DNA
mutant enzyme P210G, at pH 7.5 and 37°C
-
0.00017
cytosine in single-stranded viral DNA
mutant enzyme D370A, at pH 7.5 and 37°C
-
0.0002
cytosine in single-stranded viral DNA
mutant enzyme R256A, at pH 7.5 and 37°C
-
0.000517
cytosine in single-stranded viral DNA
mutant enzyme F268A, at pH 7.5 and 37°C
-
0.00085
cytosine in single-stranded viral DNA
mutant enzyme R376A, at pH 7.5 and 37°C
-
0.001
cytosine in single-stranded viral DNA
mutant enzyme Q380A, at pH 7.5 and 37°C
-
0.0014
cytosine in single-stranded viral DNA
mutant enzyme Q245A, at pH 7.5 and 37°C
-
0.0018
cytosine in single-stranded viral DNA
wild type enzyme, at pH 7.5 and 37°C
-
0.002
cytosine in single-stranded viral DNA
mutant enzyme D264A, at pH 7.5 and 37°C
-
0.0047
cytosine in single-stranded viral DNA
mutant enzyme H248G, at pH 7.5 and 37°C
-
0.008
cytosine in single-stranded viral DNA
mutant enzyme H250A, at pH 7.5 and 37°C
-
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0.001 - 0.24
5'-ATTCCCAATT-3'
0.0012 - 0.143
cytidine in HIV-1 virus ssDNA
-
0.0012 - 0.24
cytosine in single-stranded viral DNA
-
0.001
5'-ATTCCCAATT-3'
mutant P210A, pH 7.5, 20°C
0.001
5'-ATTCCCAATT-3'
mutant R256A, pH 7.5, 20°C
0.003
5'-ATTCCCAATT-3'
mutant R374A, pH 7.5, 20°C
0.005
5'-ATTCCCAATT-3'
mutant D264A, pH 7.5, 20°C
0.005
5'-ATTCCCAATT-3'
mutant Q245A, pH 7.5, 20°C
0.009
5'-ATTCCCAATT-3'
mutant P210G, pH 7.5, 20°C
0.014
5'-ATTCCCAATT-3'
mutant D370A, pH 7.5, 20°C
0.014
5'-ATTCCCAATT-3'
mutant R376A, pH 7.5, 20°C
0.023
5'-ATTCCCAATT-3'
mutant F268A, pH 7.5, 20°C
0.062
5'-ATTCCCAATT-3'
mutant Q380A, pH 7.5, 20°C
0.09
5'-ATTCCCAATT-3'
wild-type, pH 7.5, 20°C
0.143
5'-ATTCCCAATT-3'
mutant H248G, pH 7.5, 20°C
0.24
5'-ATTCCCAATT-3'
mutant H250A, pH 7.5, 20°C
0.0012
cytidine in HIV-1 virus ssDNA
mutant R256A, pH not specified in the publication, temperature not specified in the publication
-
0.0013
cytidine in HIV-1 virus ssDNA
mutant P210A, pH not specified in the publication, temperature not specified in the publication
-
0.0031
cytidine in HIV-1 virus ssDNA
mutant R374A, pH not specified in the publication, temperature not specified in the publication
-
0.0046
cytidine in HIV-1 virus ssDNA
mutant D264A, pH not specified in the publication, temperature not specified in the publication
-
0.005
cytidine in HIV-1 virus ssDNA
mutant Q245A, pH not specified in the publication, temperature not specified in the publication
-
0.009
cytidine in HIV-1 virus ssDNA
mutant P210G, pH not specified in the publication, temperature not specified in the publication
-
0.0135
cytidine in HIV-1 virus ssDNA
mutant R376A, pH not specified in the publication, temperature not specified in the publication
-
0.0143
cytidine in HIV-1 virus ssDNA
mutant D370A, pH not specified in the publication, temperature not specified in the publication
-
0.0228
cytidine in HIV-1 virus ssDNA
mutant F268A, pH not specified in the publication, temperature not specified in the publication
-
0.024
cytidine in HIV-1 virus ssDNA
mutant H250A, pH not specified in the publication, temperature not specified in the publication
-
0.0618
cytidine in HIV-1 virus ssDNA
mutant Q380A, pH not specified in the publication, temperature not specified in the publication
-
0.09
cytidine in HIV-1 virus ssDNA
wild-type, pH not specified in the publication, temperature not specified in the publication
-
0.143
cytidine in HIV-1 virus ssDNA
mutant H248G, pH not specified in the publication, temperature not specified in the publication
-
0.0012
cytosine in single-stranded viral DNA
mutant enzyme P210A, at pH 7.5 and 37°C
-
0.0012
cytosine in single-stranded viral DNA
mutant enzyme R256A, at pH 7.5 and 37°C
-
0.0031
cytosine in single-stranded viral DNA
mutant enzyme R374A, at pH 7.5 and 37°C
-
0.0046
cytosine in single-stranded viral DNA
mutant enzyme D264A, at pH 7.5 and 37°C
-
0.005
cytosine in single-stranded viral DNA
mutant enzyme Q245A, at pH 7.5 and 37°C
-
0.009
cytosine in single-stranded viral DNA
mutant enzyme P210G, at pH 7.5 and 37°C
-
0.0135
cytosine in single-stranded viral DNA
mutant enzyme R376A, at pH 7.5 and 37°C
-
0.01425
cytosine in single-stranded viral DNA
mutant enzyme H248G, at pH 7.5 and 37°C
-
0.0143
cytosine in single-stranded viral DNA
mutant enzyme D370A, at pH 7.5 and 37°C
-
0.023
cytosine in single-stranded viral DNA
mutant enzyme F268A, at pH 7.5 and 37°C
-
0.062
cytosine in single-stranded viral DNA
mutant enzyme Q380A, at pH 7.5 and 37°C
-
0.09
cytosine in single-stranded viral DNA
wild type enzyme, at pH 7.5 and 37°C
-
0.24
cytosine in single-stranded viral DNA
mutant enzyme H250A, at pH 7.5 and 37°C
-
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0.00059
(12bS)-5,6,6a,7,8,12b-hexahydrobenzo[a]phenanthridine-10,11-diol
Homo sapiens
at pH 7.8 and 37°C
0.0013
(1R,2S)-2-(methylamino)-1-phenylpropan-1-ol
Homo sapiens
at pH 7.8 and 37°C
0.085
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoic acid
Homo sapiens
at pH 7.8 and 37°C
0.0053
(2S)-3-(3,4-dihydroxyphenyl)-2-hydrazinyl-2-methylpropanoic acid
Homo sapiens
at pH 7.8 and 37°C
0.019
(3,4-dihydroxyphenyl)acetic acid
Homo sapiens
at pH 7.8 and 37°C
0.029
(5E)-N-methyl-2,3-diphenyl-1,2,4-thiadiazol-5(2H)-imine
Homo sapiens
at pH 7.8 and 37°C
0.0029
(6aR)-6-(prop-2-en-1-yl)-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
Homo sapiens
at pH 7.8 and 37°C
0.0013
(6aR)-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
Homo sapiens
at pH 7.8 and 37°C
0.0017
(6aR)-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-2,10,11-triol
Homo sapiens
at pH 7.8 and 37°C
0.0064
(6aR)-6-propyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-10,11-diol
Homo sapiens
at pH 7.8 and 37°C
0.0075
(6R,7R)-3-[(acetyloxy)methyl]-8-oxo-7-[2-[(pyridin-4-yl)sulfanyl]acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
Homo sapiens
at pH 7.8 and 37°C
0.027
1-phenyl-2,3,4,5-tetrahydro-1H-3-benzazepine-7,8-diol
Homo sapiens
at pH 7.8 and 37°C
0.004
2-amino-3-(2,4,5-trihydroxyphenyl)propanoic acid
Homo sapiens
at pH 7.8 and 37°C
0.003
2-Iodoacetamide
Homo sapiens
at pH 7.8 and 37°C
0.0028
2-phenyl-1,2-benzoselenazol-3(2H)-one
Homo sapiens
at pH 7.8 and 37°C
0.002
2-[(E)-2-(3,4-dihydroxyphenyl)ethenyl]-6-hydroxy-4H-pyran-4-one
Homo sapiens
at pH 7.8 and 37°C
0.00043
2-[methyl(nitroso)amino]benzene-1,4-diol
Homo sapiens
at pH 7.8 and 37°C
0.00049
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-yl)methanediyl]bis(6-hydroxybenzoic acid)
Homo sapiens
at pH 7.8 and 37°C
0.0034
3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one
Homo sapiens
at pH 7.8 and 37°C
0.0088
4,4'-(2,3-dimethylbutane-1,4-diyl)dibenzene-1,2-diol
Homo sapiens
at pH 7.8 and 37°C
0.0013
4-(4,5,6,7-tetrahydrothieno[2,3-c]pyridin-4-yl)benzene-1,2-diol
Homo sapiens
at pH 7.8 and 37°C
0.0061
4-amino-5-methyl-1,2,4-triazole-3-thiol
Homo sapiens
-
at pH 7.4 and 37°C
0.0035
4-[(2-sulfanyl-1H-imidazol-1-yl)methyl]phenol
Homo sapiens
at pH 7.8 and 37°C
0.0043
4-[(4-bromobenzylidene)amino]-1,2,4-triazole-3-thiol
Homo sapiens
-
at pH 7.4 and 37°C
0.0039
4-[(4-methoxybenzylidene)amino]-5-methyl-1,2,4-triazole-3-thiol
Homo sapiens
-
at pH 7.4 and 37°C
0.0018
4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]benzene-1,2-diol
Homo sapiens
at pH 7.8 and 37°C
0.0091
4-[methyl(nitroso)amino]benzene-1,2-diol
Homo sapiens
at pH 7.8 and 37°C
0.0007
6-amino-5,6,7,8-tetrahydronaphthalene-2,3-diol
Homo sapiens
at pH 7.8 and 37°C
0.00036
aurothio-beta-D-glucose
Homo sapiens
at pH 7.8 and 37°C
0.0026
benzene-1,4-diol
Homo sapiens
at pH 7.8 and 37°C
0.013
cephapirin
Homo sapiens
at pH 7.8 and 37°C
0.00017
cyclohexa-2,5-diene-1,4-dione
Homo sapiens
at pH 7.8 and 37°C
0.013
methyl 2-amino-3-(3,4-dihydroxyphenyl)propanoate
Homo sapiens
at pH 7.8 and 37°C
0.0082
N-(3-thio-5-methyl-1,2,4-triazol-4-yl)benzamide
Homo sapiens
-
at pH 7.4 and 37°C
0.0064
N-[(4bS,8R,8aS)-7-(cyclopropylmethyl)-1,8a-dihydroxy-5,6,7,8,8a,9,14,14b-octahydro-4,8-methano[1]benzofuro[2,3-a]pyrido[4,3-b]carbazol-11-yl]guanidine
Homo sapiens
at pH 7.8 and 37°C
0.00045
N-[2-(3,4-dihydroxyphenyl)ethyl]acetamide
Homo sapiens
at pH 7.8 and 37°C
0.00013
p-chloromercuribenzoate
Homo sapiens
at pH 7.8 and 37°C
0.0056
tetrasodium 3-[(E)-[4-formyl-5,6-dihydroxy-3-[(phosphonatoperoxy)methyl]pyridin-2-yl]diazenyl]-7-nitronaphthalene-1,5-disulfonate
Homo sapiens
at pH 7.8 and 37°C
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metabolism
the APOBEC3 family has many roles, such as restricting endogenous and exogenous retrovirus replication and retrotransposon insertion events and reducing DNA-induced inflammation
metabolism
the enzyme generates cytidine to deoxyuridine mutations in single-stranded DNA, and is capable of restricting replication of HIV-1 by generating mutations in viral genome
physiological function
APOBEC3G is a single-stranded DNA cytidine deaminase capable of restricting retroviral replication
physiological function
the enzyme causes C to T mutations in the cDNA copy of the HIV-1 genome
physiological function
the enzyme causes mutational diversity by initiating mutations on regions of single-stranded DNA. The enzyme enters the cytoplasm of the targeted T cell and catalyzes C deaminations on reverse transcribed cDNA causing HIV-1 retroviral inactivation. Enzyme-initiated mutations boost human fitness and restricts HIV-1 replication in the absence of the viral infectivity factor. The enzyme is involved in hepatic metastasis of colorectal cancer
physiological function
the enzyme exhibits anti-human immunodeficiency virus-1 (HIV-1) activity by deaminating cytidines of the minus strand of HIV-1. Virus infectivity factor of HIV-1 counteracts the anti-HIV-1 activity of the enzyme
physiological function
the enzyme inhibits HIV replication and inhibits retroviral infection by deaminating first strand cDNA, generating viral DNA mutations and potential viral elimination
physiological function
-
the enzyme is a single-stranded DNA cytosine deaminase that functions in innate immunity against retroviruses and retrotransposons. The enzyme can potently restrict virus infectivity factor-deficient HIV-1 replication by catalyzing excessive levels of G->A hypermutation. Sublethal levels of enzyme-catalyzed mutation may contribute to the high level of HIV-1 fitness and its incurable prognosis
physiological function
-
the enzyme is an endogenous inhibitor of human immunodeficiency virus type 1 (HIV-1) replication, able to induce G to A hypermutation in newly synthesized viral DNA
physiological function
-
the enzyme is an important component of the cellular innate immune response to retroviral infection. The enzyme APOBEC3G can extinguish HIV-1 infectivity by its incorporation into virus particles and subsequent cytosine deaminase activity that attacks the nascent viral cDNA during reverse transcription, causing lethal mutagenesis. The enzyme can also induce sublethal mutagenesis, which maintains virus infectivity and contribute to HIV-1 variation
physiological function
the enzyme is capable of blocking retrovirus replication by editing viral cDNA and impairing reverse transcription
physiological function
-
the enzyme is encapsulated by the HIV virion and facilitates restriction of HIV-1 infection in T cells by deaminating cytosines in nascent minus-strand complementary DNA
physiological function
the enzyme mutates the human immunodeficiency virus (HIV) genome by converting deoxycytidine to deoxyuridine in signature trinucleotides (CCC, TCC) on minus strand viral DNA during reverse transcription. The enzyme restricts viral propagation by degrading or incapacitating the coding ability of the HIV genome. The enzyme contributes to the evasion of adaptive immunity by HIV
physiological function
-
the enzyme restricts replication of HIV-1 by inducing viral genome mutagenesis through deamination of cytosine to uracil on HIV-1 cDNA processively through jumping and sliding. The jumping and sliding of Apo3G is needed for efficient mutational inactivation of HIV-1
physiological function
-
the single-stranded DNA-dependent cytosine deaminase inactivates HIV-1 in T cells by C to T hypermutation
physiological function
APOBEC3G protein inhibits HCV replication through direct binding at non-structural protein NS3 at its C-terminus, which is responsible for NS3's helicase and NTPase activities
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C243A/C321A/C356A
-
the mutation has no effect on localization, deamination, oligomerization, or HIV-1 Vif-deficient restriction capabilities. The mutant is only partially resistant to inhibitor MN256.0105, with recovered deamination efficiency of 19%
C288A/C291A
-
the mutant enzyme shows about 18% activity compared to the wild type enzyme
C321A
-
the mutation has no effect on localization, deamination, oligomerization, or HIV-1 Vif-deficient restriction capabilities. The mutant is only partially resistant to inhibitor MN256.0105, with recovered deamination efficiency of 21%
C97A/C100A
-
the mutant enzyme shows about 18% activity compared to the wild type enzyme
F202A
the mutation causes a decrease of the enzyme activity
F241K
the mutation causes a decrease of the enzyme activity
F298A
the mutant shows about 10% deamination activity compared to the wild type enzyme
H186R
-
the clinical mutant is associated with high viral loads. The mutant has altered DNA scanning properties in sliding which results in decreased abilities to induce mutagenesis during reverse transcription. The mutant retains a strong preference for deamination of the 5'-CCC motif and exhibits a processivity factor that is similar to native enzym
H250G
158% of wild-type activtiy
H257A
-
the mutant enzyme shows about 10% activity compared to the wild type enzyme
H81A
-
the mutant enzyme shows about 25% activity compared to the wild type enzyme
I314A/Y315A
-
site-directed mutagenesis, C-terminal CD2 domain mutant, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms
L235A
the mutation causes a decrease of the enzyme activity
L235K
the mutation causes a decrease of the enzyme activity
L242A
the mutation causes a decrease of the enzyme activity
L242K
the mutation causes a decrease of the enzyme activity
N244A
the mutant shows no deamination activity
R213E
the mutant shows about 3% deamination activity compared to the wild type enzyme
R215E
the mutant shows no deamination activity
R256E
the mutant shows about 3% deamination activity compared to the wild type enzyme
R313A/D316A/D317A/Q318A
-
site-directed mutagenesis, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms
R313E/R320D
the mutant shows no deamination activity and about 75% single-stranded DNA binding compared to the wild type enzyme
R374E/R376D
the mutant shows less than 10% deamination activity and about 50% single-stranded DNA binding compared to the wild type enzyme
T203A
the mutation causes a decrease of the enzyme activity
V233A
the mutation causes a decrease of the enzyme activity
V233K
the mutation causes a decrease of the enzyme activity
W232A
the mutation causes a decrease of the enzyme activity
W285A
the mutant shows no deamination activity
Y124A/Y125A
-
site-directed mutagenesis, the N-terminal CD1 domain mutant is composed of roughly 47% monomers, 42% dimers, 10% tetramers, and 1% much larger molecular mass species of about 650 kDa
Y315A
the mutant shows no deamination activity
E259Q
-
site-directed mutagenesis
T218A
-
site-directed mutagenesis
T218E
-
site-directed mutagenesis
T27A
-
site-directed mutagenesis
T27E
-
site-directed mutagenesis
D264A
the variant has 5% of the catalytic efficiency of the wild type protein
D264A
5.1% of wild-type activity
D264A
5.1% of wild-type activtiy
D316R/D317R
the mutant shows about 180% deamination activity and about 200% single-stranded DNA binding compared to the wild type enzyme
D316R/D317R
-
the mutations increase affinity for substrate and deamination specificity
D370A
15.8% of wild-type activity
D370A
the variant has 16% of the catalytic efficiency of the wild type protein
D370A
15.8% of wild-type activtiy
F126A/W127A
-
site-directed mutagenesis, the N-terminal CD1 domain mutant, that shows disrupted dimerization at the predicted CD1-CD1 dimer interface, predominantly converts Apo3G to a monomer that binds single-stranded DNA, Alu RNA, and catalyzes processive C to U deaminations with 3'-5' deamination polarity, similar to wild-type Apo3G. The mutation causes severe disruption in oligomer formation resulting in about 92% monomers and 8% dimers, with no larger oligomer forms detected
F126A/W127A
-
the mutant has altered DNA scanning properties in jumping which results in decreased abilities to induce mutagenesis during reverse transcription. The mutant demonstrates a stronger preference than native enzyme for C residues at the 5'-ssDNA end and is processive
F126A/W127A
the mutant interferes with head-to-head dimerization but retains many of the salient biochemical properties observed in the native protein
F268A
the variant has 25% of the catalytic efficiency of the wild type protein
F268A
25.2% of wild-type activity
F268A
25.2% of wild-type activtiy
H248G
the variant has 158% of the catalytic efficiency of the wild type protein
H248G
158% of wild-type activity
H250A
the variant has 266% of the catalytic efficiency of the wild type protein
H250A
266% of wild-type activity
H250A
266% of wild-type activtiy
P210A
1.4% of wild-type activity
P210A
the variant has 1% of the catalytic efficiency of the wild type protein
P210A
1.4% of wild-type activtiy
P210G
the variant has 10% of the catalytic efficiency of the wild type protein
P210G
9.9% of wild-type activity
P210G
9.9% of wild-type activtiy
Q245A
the mutation nearly abolishes the catalytic efficiency to 5% compared to the wild type protein
Q245A
5.5% of wild-type activity
Q245A
5.5% of wild-type activtiy
Q380A
the variant has 68% of the catalytic efficiency of the wild type protein
Q380A
68.5% of wild-type activity
Q380A
68.5% of wild-type activtiy
R256A
1.3% of wild-type activity
R256A
the mutation nearly abolishes the catalytic efficiency to 1% compared to the wild type protein
R256A
1.3% of wild-type activtiy
R374A
3.4% of wild-type activity
R374A
the variant has 3% of the catalytic efficiency of the wild type protein
R374A
3.4% of wild-type activtiy
R376A
14.9% of wild-type activity
R376A
the variant has 15% of the catalytic efficiency of the wild type protein
R376A
14.9% of wild-type activtiy
additional information
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CD2-2, possessing the deamination activity, incorporated efficiently into HIV-1 is unable to mutate viral cDNA. Construction of three A3G mutants CD1-1, CD2-2 and CD2-1, which contain duplicate CD1 domain, duplicate CD2 domain, and position switched CD domain, respectively. The two CD domains are functionally equivalent in virion encapsidation and the interaction with HIV-1 Vif of hA3G, whereas CD domain switch or replacement greatly affect the sensitivity to Vif-induced degradation, editing and antiviral activity of hA3G. The switch of the CD domain affects nucleotide sequence preference pattern of the deaminase. The mutants show a nucleotide sequence preference pattern
additional information
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comparison of Apo3G native and monomeric N-mutant F/W ssDNA substrate binding and catalysis, overview
additional information
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phospho-mimetic mutations inhibit DNA cytidine deaminase activity
additional information
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phospho-mimetic mutations inhibit DNA cytidine deaminase activity
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Chelico, L.; Prochnow, C.; Erie, D.A.; Chen, X.S.; Goodman, M.F.
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Homo sapiens
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Homo sapiens (Q9HC16)
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DNA Repair
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2010
Homo sapiens (Q9HC16)
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Demorest, Z.L.; Li, M.; Harris, R.S.
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Homo sapiens, Mus musculus
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Homo sapiens
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Functional analysis of the two cytidine deaminase domains in APOBEC3G
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2011
Homo sapiens
brenda
Shlyakhtenko, L.S.; Lushnikov, A.Y.; Miyagi, A.; Li, M.; Harris, R.S.; Lyubchenko, Y.L.
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51
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2012
Homo sapiens (Q9HC16)
brenda
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2013
Homo sapiens (Q9HC16), Homo sapiens
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ChemMedChem
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2012
Homo sapiens
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Coker, H.A.; Petersen-Mahrt, S.K.
The nuclear DNA deaminase AID functions distributively whereas cytoplasmic APOBEC3G has a processive mode of action
DNA Repair
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2006
Homo sapiens (Q9HC16)
brenda
Pham, P.; Chelico, L.; Goodman, M.F.
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DNA Repair
6
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2007
Homo sapiens (Q9HC16)
brenda
Furukawa, A.; Nagata, T.; Matsugami, A.; Habu, Y.; Sugiyama, R.; Hayashi, F.; Kobayashi, N.; Yokoyama, S.; Takaku, H.; Katahira, M.
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2009
Homo sapiens (Q9HC16)
brenda
Rausch, J.W.; Chelico, L.; Goodman, M.F.; Le Grice, S.F.
Dissecting APOBEC3G substrate specificity by nucleoside analog interference
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284
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2009
Homo sapiens
brenda
Feng, Y.; Chelico, L.
Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain
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2011
Homo sapiens
brenda
Sadler, H.A.; Stenglein, M.D.; Harris, R.S.; Mansky, L.M.
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J. Virol.
84
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2012
Homo sapiens
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Chelico, L.; Pham, P.; Calabrese, P.; Goodman, M.F.
APOBEC3G DNA deaminase acts processively 3' -> 5' on single-stranded DNA
Nat. Struct. Mol. Biol.
13
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2006
Homo sapiens
brenda
Zhang, H.; Yang, B.; Pomerantz, R.J.; Zhang, C.; Arunachalam, S.C.; Gao, L.
The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
Nature
424
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2003
Homo sapiens
brenda
Holden, L.G.; Prochnow, C.; Chang, Y.P.; Bransteitter, R.; Chelico, L.; Sen, U.; Stevens, R.C.; Goodman, M.F.; Chen, X.S.
Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications
Nature
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2008
Homo sapiens (Q9HC16)
brenda
Suspene, R.; Sommer, P.; Henry, M.; Ferris, S.; Guetard, D.; Pochet, S.; Chester, A.; Navaratnam, N.; Wain-Hobson, S.; Vartanian, J.P.
APOBEC3G is a single-stranded DNA cytidine deaminase and functions independently of HIV reverse transcriptase
Nucleic Acids Res.
32
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2004
Homo sapiens (Q9HC16)
brenda
Monajemi, M.; Woodworth, C.F.; Benkaroun, J.; Grant, M.; Larijani, M.
Emerging complexities of APOBEC3G action on immunity and viral fitness during HIV infection and treatment
Retrovirology
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35
2012
Homo sapiens (Q9HC16)
brenda
Lu, X.; Zhang, T.; Xu, Z.; Liu, S.; Zhao, B.; Lan, W.; Wang, C.; Ding, J.; Cao, C.
Crystal structure of DNA cytidine deaminase ABOBEC3G catalytic deamination domain suggests a binding mode of full-length enzyme to single-stranded DNA
J. Biol. Chem.
290
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2015
Homo sapiens (Q9HC16)
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Holtz, C.M.; Sadler, H.A.; Mansky, L.M.
APOBEC3G cytosine deamination hotspots are defined by both sequence context and single-stranded DNA secondary structure
Nucleic Acids Res.
41
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2013
Homo sapiens (Q9HC16)
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Zhu, Y.P.; Peng, Z.G.; Wu, Z.Y.; Li, J.R.; Huang, M.H.; Si, S.Y.; Jiang, J.D.
Host APOBEC3G protein inhibits HCV replication through direct binding at NS3
PLoS ONE
10
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2015
Homo sapiens (Q9HC16)
brenda
Lu, X.; Zhang, T.; Xu, Z.; Liu, S.; Zhao, B.; Lan, W.; Wang, C.; Ding, J.; Cao, C.
Crystal structure of DNA cytidine deaminase ABOBEC3G catalytic deamination domain suggests a binding mode of full-length enzyme to single-stranded DNA
J. Biol. Chem.
290
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2015
Homo sapiens (Q9HC16)
brenda
Adolph, M.B.; Love, R.P.; Chelico, L.
Biochemical basis of APOBEC3 deoxycytidine deaminase activity on diverse DNA substrates
ACS Infect. Dis.
4
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2018
Homo sapiens (Q9HC16)
brenda
Ito, F.; Fu, Y.; Kao, S.A.; Yang, H.; Chen, X.S.
Family-wide comparative analysis of cytidine and methylcytidine deamination by eleven human APOBEC proteins
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Homo sapiens (Q9HC16)
brenda
Maiti, A.; Myint, W.; Kanai, T.; Delviks-Frankenberry, K.; Sierra Rodriguez, C.; Pathak, V.K.; Schiffer, C.A.; Matsuo, H.
Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with sDNA
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Homo sapiens (Q9HC16)
brenda
Wang, Y.; Wu, S.; Zheng, S.; Wang, S.; Wali, A.; Ezhilarasan, R.; Sulman, E.P.; Koul, D.; Alfred Yung, W.K.
APOBEC3G acts as a therapeutic target in mesenchymal gliomas by sensitizing cells to radiation-induced cell death
Oncotarget
8
54285-54296
2017
Homo sapiens (Q9HC16), Homo sapiens
brenda
Kamba, K.; Nagata, T.; Katahira, M.
Catalytic analysis of APOBEC3G involving real-time NMR spectroscopy reveals nucleic acid determinants for deamination
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Homo sapiens (Q9HC16)
brenda