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Information on EC 3.5.4.B9 - cytosine deaminase APOBEC3G and Organism(s) Homo sapiens and UniProt Accession Q9HC16
for references in articles please use BRENDA:EC3.5.4.B9preliminary BRENDA-supplied EC number
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3.5.4.B9 cytosine deaminase APOBEC3GSpecify your search results
Word Map
- 3.5.4.B9
-
deamination
- virion
-
hypermutation
- retroviruses
- deaminases
- lentiviruses
-
encapsidation
-
activation-induced
-
minus-strand
-
vif-defective
-
class-switched
-
g-to-a
-
vif-induced
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
cytosine in single-stranded viral DNA
+
=
uracil in single-stranded viral DNA
+
Synonyms
apo3g, dna cytidine deaminase, cem15, cytosine deaminase apobec3g, apobec 3g, apobec3g cytidine deaminase, abobec3g, apobec3g dna deaminase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
APOBEC3G
-
SYSTEMATIC NAME
IUBMB Comments
single-stranded DNA cytosine aminohydrolase APOBEC3G
-
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
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
-
-
-
?
deoxycytosine in single-stranded viral DNA + H2O
deoxyuridine in single-stranded viral DNA + NH3
-
-
-
?
TTTCCCCGC + H2O
TTTCCUCGC + NH3
sequence with highest deamination rate
-
-
?
5'-AAAGAGAAAGAGAAACCCAAAGAGGAAAGGTGAGGAGAA-3' + H2O
5'-AAAGAGAAAGAGAAACCUAAAGAGGAAAGGTGAGGAGAA-3' + NH3
-
the enzyme targets 5'-CCCA-3' sequences with 5'-AAACCCAAA-3' recognized most efficiently
-
-
?
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 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
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 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
-
-
?
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
-
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 targets 5'-CCCA-3' sequences with 5'-AAACCCAAA-3' recognized most efficiently
-
-
?
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 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
-
-
?
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 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
-
-
?
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
deoxycytosine in single-stranded viral DNA + H2O
deoxyuridine in single-stranded viral 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 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
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 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
-
-
?
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
-
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 targets 5'-CCCA-3' sequences with 5'-AAACCCAAA-3' recognized most efficiently
-
-
?
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 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 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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Mg2+
-
large increase in the mobility of APOBEC3G cytidine deaminase on ssDNA at higher salt, Mg2+ or NaCl
NaCl
-
large increase in the mobility of APOBEC3G cytidine deaminase on ssDNA at higher salt, Mg2+ or NaCl
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
-
3,3'-[(3-carboxy-4-oxocyclohexa-2,5-dien-1-yl)methanediyl]bis(6-hydroxybenzoic acid)
-
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
-
tetrasodium 3-[(E)-[4-formyl-5,6-dihydroxy-3-[(phosphonatoperoxy)methyl]pyridin-2-yl]diazenyl]-7-nitronaphthalene-1,5-disulfonate
-
4-[(4-bromobenzylidene)amino]-1,2,4-triazole-3-thiol
-
MN256.0105, 99% inhibition at 0.02 mM
additional information
the virion infectivity factor of HIV binds cytoplasmic enzyme marking it for degradation
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
large increase in the mobility of APOBEC3G cytidine deaminase on ssDNA at higher salt, Mg2+ or NaCl
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pre-steady state and steady state kinetics, stopped-flow fluorescence measurements, detailed overview
-
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00059
(12bS)-5,6,6a,7,8,12b-hexahydrobenzo[a]phenanthridine-10,11-diol
Homo sapiens
at pH 7.8 and 37°C
0.0053
(2S)-3-(3,4-dihydroxyphenyl)-2-hydrazinyl-2-methylpropanoic 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
0.002
2-[(E)-2-(3,4-dihydroxyphenyl)ethenyl]-6-hydroxy-4H-pyran-4-one
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
0.0018
4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]benzene-1,2-diol
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
0.0064
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
0.0056
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
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
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
APOBEC3G is preferentially expressed in mesenchymal gliomas
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
physiological function
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 capable of blocking retrovirus replication by editing viral cDNA and impairing reverse transcription
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
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
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 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 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
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
-
x * 46000, the enzyme is active in monomeric, dimeric, and larger oligomeric states
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer or dimer
-
x * 46000, the enzyme is active in monomeric, dimeric, and larger oligomeric states
additional information
additional information
the enzyme is a mix of monomers, dimers, and higher order oligomers
additional information
-
the enzyme is a mix of monomers, dimers, and higher order oligomers
additional information
-
A3G contains two cytidine deaminase domains. The CD2 domain possesses the deamination activity
additional information
-
Apo3G has a catalytically inactive N-terminal CD1 domain and an active C-terminal CD2 domain. Apo3G exists as monomers, dimers, tetramers, and higher order oligomers whose distributions depend on DNA substrate and salt
additional information
-
APOBEC3G cytidine deaminase catalytically inactive N-terminal CD1 domain has a predicted large net positive charge, in contrast to the catalytically active CD2 domain, and is likely to govern the mobility of APOBEC3G cytidine deaminase on ssDNA, which should depend on metal ion concentration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
carboxy-terminal deaminase domain 2 of APOBEC3G (residues 197-380), hanging drop vapor diffusion method, using 100 mM MES, pH 6.5, 40% (w/v) PEG 200, at 18°C
head-to-tail dimer of the A3G catalytic deamination domain A3G-CD2, sitting drop vapor diffusion method, using 0.1 M sodium citrate tribasic dehydrate, pH 5.6, 20% (v/v) 2-propanol, 20% (w/v) polyethylene glycol 4000
sitting drop vapor diffusion method at 4°C, crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA at 1.86 A resolution
structure of a A3G-CD2 head-to-tail dimer in which the N terminus of the monomer H (head) interacts with the C terminus of monomer T (tail). A continuous DNA binding groove is observed
structure of a novel catalytic domain head-to-tail dimer in which the N terminus of the monomer head
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D264A
D316R/D317R
the mutant shows about 180% deamination activity and about 200% single-stranded DNA binding compared to the wild type enzyme
D370A
F126A/W127A
the mutant interferes with head-to-head dimerization but retains many of the salient biochemical properties observed in the native protein
F268A
F298A
the mutant shows about 10% deamination activity compared to the wild type enzyme
H248G
H250A
P210A
P210G
Q245A
Q380A
R213E
the mutant shows about 3% deamination activity compared to the wild type enzyme
R256A
R256E
the mutant shows about 3% deamination activity compared to the wild type enzyme
R313E/R320D
the mutant shows no deamination activity and about 75% single-stranded DNA binding compared to the wild type enzyme
R374A
R374E/R376D
the mutant shows less than 10% deamination activity and about 50% single-stranded DNA binding compared to the wild type enzyme
R376A
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
D316R/D317R
-
the mutations increase affinity for substrate and deamination specificity
F126A/W127A
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
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
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
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
additional information
D264A
the variant has 5% of the catalytic efficiency of the wild type protein
D370A
the variant has 16% of the catalytic efficiency of the wild type protein
F268A
the variant has 25% of the catalytic efficiency of the wild type protein
H248G
the variant has 158% of the catalytic efficiency of the wild type protein
H250A
the variant has 266% of the catalytic efficiency of the wild type protein
P210A
the variant has 1% of the catalytic efficiency of the wild type protein
P210G
the variant has 10% of the catalytic efficiency of the wild type protein
Q245A
the mutation nearly abolishes the catalytic efficiency to 5% compared to the wild type protein
Q380A
the variant has 68% of the catalytic efficiency of the wild type protein
R256A
the mutation nearly abolishes the catalytic efficiency to 1% compared to the wild type protein
R374A
the variant has 3% of the catalytic efficiency of the wild type protein
R376A
the variant has 15% of the catalytic efficiency of the wild type protein
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
additional information
-
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
-
comparison of Apo3G native and monomeric N-mutant F/W ssDNA substrate binding and catalysis, overview
additional information
-
phospho-mimetic mutations inhibit DNA cytidine deaminase activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose column chromatography and MonoQ column chromatography
glutathione-Sepharose resin column chromatography and DEAE FF column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the carboxyl-terminal catalytic domain is expressed in Escherichia coli BL-21 DE3 codon+RIL cells
expression of activation-induced deaminase, i.e. AID, and APOBEC3G in Escherichia coli strain BW310 and in human HEK293T cells
-
incorporation of hA3G CD1 and CD2 domain mutants into HIV-1. Cotransfection of plasmids coding HIV-1 vif and plasmids containing either wild-type or mutant hA3G in 293T cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
APOBEC3G mediated checkpoint activation through checkpoint kinase 2 (Chk2) is one of the critical regulatory mechanisms that underlies the preferential DNA damage checkpoint response and radioresistance of Glioma Initiating Cells. Thus, anti-APOBEC3G therapy may synergize with radiotherapy and other current treatments to overcome the therapeutic resistance of gliomas. APOBEC3G represents a potential molecular target for novel therapeutics that will improve the treatment outcome of glioma patients
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chelico, L.; Prochnow, C.; Erie, D.A.; Chen, X.S.; Goodman, M.F.
Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G
J. Biol. Chem.
285
16195-16205
2010
Homo sapiens
Li, M.; Shandilya, S.M.; Carpenter, M.A.; Rathore, A.; Brown, W.L.; Perkins, A.L.; Harki, D.A.; Solberg, J.; Hook, D.J.; Pandey, K.K.; Parniak, M.A.; Johnson, J.R.; Krogan, N.J.; Somasundaran, M.; Ali, A.; Schiffer, C.A.; Harris, R.S.
First-in-class small molecule inhibitors of the single-strand DNA cytosine deaminase APOBEC3G
ACS Chem. Biol.
7
506-517
2012
Homo sapiens (Q9HC16)
Carpenter, M.A.; Rajagurubandara, E.; Wijesinghe, P.; Bhagwat, A.S.
Determinants of sequence-specificity within human AID and APOBEC3G
DNA Repair
9
579-587
2010
Homo sapiens (Q9HC16)
Demorest, Z.L.; Li, M.; Harris, R.S.
Phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein
J. Biol. Chem.
286
26568-26575
2011
Homo sapiens, Mus musculus
Senavirathne, G.; Jaszczur, M.; Auerbach, P.A.; Upton, T.G.; Chelico, L.; Goodman, M.F.; Rueda, D.
Single-stranded DNA scanning and deamination by APOBEC3G cytidine deaminase at single molecule resolution
J. Biol. Chem.
287
15826-15835
2012
Homo sapiens
Li, X.; Ma, J.; Zhang, Q.; Zhou, J.; Yin, X.; Zhai, C.; You, X.; Yu, L.; Guo, F.; Zhao, L.; Li, Z.; Zeng, Y.; Cen, S.
Functional analysis of the two cytidine deaminase domains in APOBEC3G
Virology
414
130-136
2011
Homo sapiens
Shlyakhtenko, L.S.; Lushnikov, A.Y.; Miyagi, A.; Li, M.; Harris, R.S.; Lyubchenko, Y.L.
Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA
Biochemistry
51
6432-6440
2012
Homo sapiens (Q9HC16)
Jaszczur, M.; Bertram, J.G.; Pham, P.; Scharff, M.D.; Goodman, M.F.
AID and Apobec3G haphazard deamination and mutational diversity
Cell. Mol. Life Sci.
70
3089-3108
2013
Homo sapiens (Q9HC16), Homo sapiens
Olson, M.E.; Li, M.; Harris, R.S.; Harki, D.A..
Small-molecule APOBEC3G DNA cytosine deaminase inhibitors based on a 4-amino-1,2,4-triazole-3-thiol scaffold
ChemMedChem
8
112-117
2012
Homo sapiens
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
6
235-243
2006
Homo sapiens (Q9HC16)
Pham, P.; Chelico, L.; Goodman, M.F.
DNA deaminases AID and APOBEC3G act processively on single-stranded DNA
DNA Repair
6
689-692
2007
Homo sapiens (Q9HC16)
Furukawa, A.; Nagata, T.; Matsugami, A.; Habu, Y.; Sugiyama, R.; Hayashi, F.; Kobayashi, N.; Yokoyama, S.; Takaku, H.; Katahira, M.
Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G
EMBO J.
28
440-451
2009
Homo sapiens (Q9HC16)
Rausch, J.W.; Chelico, L.; Goodman, M.F.; Le Grice, S.F.
Dissecting APOBEC3G substrate specificity by nucleoside analog interference
J. Biol. Chem.
284
7047-7058
2009
Homo sapiens
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
J. Biol. Chem.
286
11415-11426
2011
Homo sapiens
Sadler, H.A.; Stenglein, M.D.; Harris, R.S.; Mansky, L.M.
APOBEC3G contributes to HIV-1 variation through sublethal mutagenesis
J. Virol.
84
7396-7404
2012
Homo sapiens
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
392-399
2006
Homo sapiens
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
94-98
2003
Homo sapiens
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
456
121-124
2008
Homo sapiens (Q9HC16)
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
2421-2429
2004
Homo sapiens (Q9HC16)
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
9
35
2012
Homo sapiens (Q9HC16)
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
4010-4021
2015
Homo sapiens (Q9HC16)
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
6139-6148
2013
Homo sapiens (Q9HC16)
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
e0121608
2015
Homo sapiens (Q9HC16)
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
4010-4021
2015
Homo sapiens (Q9HC16)
Adolph, M.B.; Love, R.P.; Chelico, L.
Biochemical basis of APOBEC3 deoxycytidine deaminase activity on diverse DNA substrates
ACS Infect. Dis.
4
224-238
2018
Homo sapiens (Q9HC16)
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
J. Mol. Biol.
429
1787-1799
2017
Homo sapiens (Q9HC16)
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
Nat. Commun.
9
2460
2018
Homo sapiens (Q9HC16)
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
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