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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.
    View publication on PubMedView publication on EuropePMC

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
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Organism

EC Number Organism UniProt Comment Textmining
3.5.4.B9 Homo sapiens Q9HC16
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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
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Synonyms

EC Number Synonyms Comment Organism
3.5.4.B9 APOBEC3G
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Homo sapiens