3.5.4.B9: cytosine deaminase APOBEC3G
This is an abbreviated version!
For detailed information about cytosine deaminase APOBEC3G, go to the full flat file.
Word Map on EC 3.5.4.B9
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3.5.4.B9
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deamination
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virion
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hypermutation
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retroviruses
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deaminases
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lentiviruses
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encapsidation
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activation-induced
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minus-strand
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vif-defective
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class-switched
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g-to-a
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vif-induced
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medicine
- 3.5.4.B9
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deamination
- virion
-
hypermutation
- retroviruses
- deaminases
- lentiviruses
-
encapsidation
-
activation-induced
-
minus-strand
-
vif-defective
-
class-switched
-
g-to-a
-
vif-induced
- medicine
Reaction
Synonyms
A3G, ABOBEC3G, activation-induced deaminase, Apo3G, Apobec 3G, APOBEC3G, APOBEC3G cytidine deaminase, APOBEC3G DNA deaminase, apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G, apolipoprotein B mRNA-editing enzyme, catalytic polypeptide-like 3G, apolipoprotein B mRNA-editing, enzyme-catalytic, polypeptide-like 3G, CEM15, DNA cytidine deaminase, More, single-stranded DNA deoxycytidine deaminase, single-stranded DNA-dependent deoxycytidine deaminase, ssDNA deoxycytidine deaminase
ECTree
3.5.4.B9 cytosine deaminase APOBEC3GAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.5.4.B9 - cytosine deaminase APOBEC3G
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
deoxycytosine in single-stranded viral DNA + H2O
deoxyuridine in single-stranded viral DNA + NH3
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?
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
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-
?
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
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?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
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-
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?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
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-
-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
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-
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?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
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-
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?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
cytosine deamination occurs preferentially in CpC (5'GpG/CpC5')
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-
?
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
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-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
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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
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-
?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
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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
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?
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
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-
?
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
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?
cytosine in single-stranded viral DNA + H2O
uracil in single-stranded viral DNA + NH3
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the enzyme targets 5'-CCCA-3' sequences with 5'-AAACCCAAA-3' recognized most efficiently
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?
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
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?
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
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-
?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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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?
