EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
   3.5.4.B9 | 2'-deoxycytidine + H2O |
in ssDNA |
Homo sapiens |
2'-deoxyuridine + NH3 |
- |
? |
| 3.5.4.B9 | 5'-AAAGAGAAAGAGAAACCCAAAGAGGAAAGGTGAGGAGAA-3' + H2O |
the enzyme targets 5'-CCCA-3' sequences with 5'-AAACCCAAA-3' recognized most efficiently |
Homo sapiens |
5'-AAAGAGAAAGAGAAACCUAAAGAGGAAAGGTGAGGAGAA-3' + NH3 |
- |
? |
| 3.5.4.B9 | 5'-ATTCCCAATT-3' + H2O |
- |
Homo sapiens |
5'-ATTCCUAATT-3' |
- |
? |
| 3.5.4.B9 | 5-methylcytosine in single-stranded DNA + H2O |
the enzyme exhibits low activity toward 5-methylcytosine n single-stranded DNA |
Homo sapiens |
? |
- |
? |
| 3.5.4.B9 | more |
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 |
Homo sapiens |
? |
- |
? |
| 3.5.4.B9 | more |
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 |
Homo sapiens |
? |
- |
? |
| 3.5.4.B9 | more |
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 |
Homo sapiens |
? |
- |
? |
| 3.5.4.B9 | more |
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 |
Homo sapiens |
? |
- |
? |
| 3.5.4.B9 | more |
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 |
Homo sapiens |
? |
- |
? |
| 3.5.4.B9 | more |
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 |
Homo sapiens |
? |
- |
? |
