EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.4.B9 | expressed in Sf9 insect cells | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.4.B9 | 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 | Homo sapiens |
3.5.4.B9 | 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 | 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 | 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 | uracil in single-stranded viral DNA + NH3 | - |
? | |
3.5.4.B9 | additional information | Homo sapiens | 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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.4.B9 | Homo sapiens | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
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 | 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 | Homo sapiens | uracil in single-stranded viral DNA + NH3 | - |
? | |
3.5.4.B9 | 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 | Homo sapiens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.4.B9 | Apo3G | - |
Homo sapiens |
3.5.4.B9 | APOBEC3G | - |
Homo sapiens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.4.B9 | 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 | Homo sapiens |