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Literature summary extracted from

  • Chelico, L.; Prochnow, C.; Erie, D.A.; Chen, X.S.; Goodman, M.F.
    Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G (2010), J. Biol. Chem., 285, 16195-16205.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.5.4.B9 F126A/W127A site-directed mutagenesis, the N-terminal CD1 domain mutant, that shows disrupted dimerization at the predicted CD1-CD1 dimer interface, predominantly converts Apo3G to a monomer that binds single-stranded DNA, Alu RNA, and catalyzes processive C to U deaminations with 3'-5' deamination polarity, similar to wild-type Apo3G. The mutation causes severe disruption in oligomer formation resulting in about 92% monomers and 8% dimers, with no larger oligomer forms detected Homo sapiens
3.5.4.B9 I314A/Y315A site-directed mutagenesis, C-terminal CD2 domain mutant, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms Homo sapiens
3.5.4.B9 additional information comparison of Apo3G native and monomeric N-mutant F/W ssDNA substrate binding and catalysis, overview Homo sapiens
3.5.4.B9 R313A/D316A/D317A/Q318A site-directed mutagenesis, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms Homo sapiens
3.5.4.B9 Y124A/Y125A site-directed mutagenesis, the N-terminal CD1 domain mutant is composed of roughly 47% monomers, 42% dimers, 10% tetramers, and 1% much larger molecular mass species of about 650 kDa Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.4.B9 additional information
-
 additional information pre-steady state and steady state kinetics, stopped-flow fluorescence measurements, detailed overview Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.4.B9 2'-deoxycytidine + H2O Homo sapiens in ssDNA 2'-deoxyuridine + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.B9 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.B9 2'-deoxycytidine + H2O in ssDNA Homo sapiens 2'-deoxyuridine + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.4.B9 More Apo3G has a catalytically inactive N-terminal CD1 domain and an active C-terminal CD2 domain. Apo3G exists as monomers, dimers, tetramers, and higher order oligomers whose distributions depend on DNA substrate and salt Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.5.4.B9 Apo3G
-
 Homo sapiens
3.5.4.B9 APOBEC3G
-
 Homo sapiens
3.5.4.B9 single-stranded DNA deoxycytidine deaminase
-
 Homo sapiens
3.5.4.B9 single-stranded DNA-dependent deoxycytidine deaminase
-
 Homo sapiens
3.5.4.B9 ssDNA deoxycytidine deaminase
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.4.B9 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.4.B9 7.3
-
 assay at Homo sapiens