EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.4.B9 | expressed in baculovirus-infected sf9 insect cells | Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.5.4.B9 | 88000 | - |
gel filtration | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.4.B9 | cytosine in single-stranded viral DNA + H2O | Homo sapiens | - |
uracil in single-stranded viral DNA + NH3 | - |
? | |
3.5.4.B9 | additional information | Homo sapiens | 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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.4.B9 | Homo sapiens | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.4.B9 | cytosine in single-stranded viral DNA + H2O | - |
Homo sapiens | uracil in single-stranded viral DNA + NH3 | - |
? | |
3.5.4.B9 | 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 | Homo sapiens | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.4.B9 | dimer | - |
Homo sapiens |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.4.B9 | APOBEC3G DNA deaminase | - |
Homo sapiens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.4.B9 | 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 | Homo sapiens |