Literature summary extracted from
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 (2008), Nature, 456, 121-124.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.5.4.B9 |
expressed in Escherichia coli BL21(DE3) cells and in Sf9 insect cells |
Homo sapiens |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.5.4.B9 |
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 |
Homo sapiens |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.5.4.B9 |
D316R/D317R |
the mutant shows about 180% deamination activity and about 200% single-stranded DNA binding compared to the wild type enzyme |
Homo sapiens |
3.5.4.B9 |
F298A |
the mutant shows about 10% deamination activity compared to the wild type enzyme |
Homo sapiens |
3.5.4.B9 |
N244A |
the mutant shows no deamination activity |
Homo sapiens |
3.5.4.B9 |
R213E |
the mutant shows about 3% deamination activity compared to the wild type enzyme |
Homo sapiens |
3.5.4.B9 |
R215E |
the mutant shows no deamination activity |
Homo sapiens |
3.5.4.B9 |
R256E |
the mutant shows about 3% deamination activity compared to the wild type enzyme |
Homo sapiens |
3.5.4.B9 |
R313E/R320D |
the mutant shows no deamination activity and about 75% single-stranded DNA binding compared to the wild type enzyme |
Homo sapiens |
3.5.4.B9 |
R374E/R376D |
the mutant shows less than 10% deamination activity and about 50% single-stranded DNA binding compared to the wild type enzyme |
Homo sapiens |
3.5.4.B9 |
W285A |
the mutant shows no deamination activity |
Homo sapiens |
3.5.4.B9 |
Y315A |
the mutant shows no deamination activity |
Homo sapiens |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.5.4.B9 |
Zn2+ |
contains a zinc atom in the active site |
Homo sapiens |
|
Natural Substrates/ Products (Substrates)
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 |
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 |
uracil in single-stranded viral DNA + NH3 |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.5.4.B9 |
Homo sapiens |
Q9HC16 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.5.4.B9 |
Superdex 75 gel filtration |
Homo sapiens |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.5.4.B9 |
cytosine in single-stranded viral DNA + H2O |
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 |
Homo sapiens |
uracil in single-stranded viral DNA + NH3 |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.5.4.B9 |
APOBEC3G |
- |
Homo sapiens |