3.5.4.B9	C243A/C321A/C356A	the mutation has no effect on localization, deamination, oligomerization, or HIV-1 Vif-deficient restriction capabilities. The mutant is only partially resistant to inhibitor MN256.0105, with recovered deamination efficiency of 19%	722064	
3.5.4.B9	C288A/C291A	the mutant enzyme shows about 18% activity compared to the wild type enzyme	723260	
3.5.4.B9	C321A	the mutation has no effect on localization, deamination, oligomerization, or HIV-1 Vif-deficient restriction capabilities. The mutant is only partially resistant to inhibitor MN256.0105, with recovered deamination efficiency of 21%	722064	
3.5.4.B9	C97A/C100A	the mutant enzyme shows about 18% activity compared to the wild type enzyme	723260	
3.5.4.B9	D264A	5.1% of wild-type activity	754123	
3.5.4.B9	D264A	5.1% of wild-type activtiy	754123	
3.5.4.B9	D264A	the variant has 5% of the catalytic efficiency of the wild type protein	734319	
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	723261	
3.5.4.B9	D316R/D317R	the mutations increase affinity for substrate and deamination specificity	722665	
3.5.4.B9	D370A	15.8% of wild-type activity	754123	
3.5.4.B9	D370A	15.8% of wild-type activtiy	754123	
3.5.4.B9	D370A	the variant has 16% of the catalytic efficiency of the wild type protein	734319	
3.5.4.B9	E259Q	site-directed mutagenesis	719945	
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	712428	
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	722698	
3.5.4.B9	F126A/W127A	the mutant interferes with head-to-head dimerization but retains many of the salient biochemical properties observed in the native protein	721999	
3.5.4.B9	F202A	the mutation causes a decrease of the enzyme activity	722114	
3.5.4.B9	F241K	the mutation causes a decrease of the enzyme activity	722114	
3.5.4.B9	F268A	25.2% of wild-type activity	754123	
3.5.4.B9	F268A	25.2% of wild-type activtiy	754123	
3.5.4.B9	F268A	the variant has 25% of the catalytic efficiency of the wild type protein	734319	
3.5.4.B9	F298A	the mutant shows about 10% deamination activity compared to the wild type enzyme	723261	
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	722698	
3.5.4.B9	H248G	158% of wild-type activity	754123	
3.5.4.B9	H248G	the variant has 158% of the catalytic efficiency of the wild type protein	734319	
3.5.4.B9	H250A	266% of wild-type activity	754123	
3.5.4.B9	H250A	266% of wild-type activtiy	754123	
3.5.4.B9	H250A	the variant has 266% of the catalytic efficiency of the wild type protein	734319	
3.5.4.B9	H250G	158% of wild-type activtiy	754123	
3.5.4.B9	H257A	the mutant enzyme shows about 10% activity compared to the wild type enzyme	723260	
3.5.4.B9	H81A	the mutant enzyme shows about 25% activity compared to the wild type enzyme	723260	
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	712428	
3.5.4.B9	L235A	the mutation causes a decrease of the enzyme activity	722114	
3.5.4.B9	L235K	the mutation causes a decrease of the enzyme activity	722114	
3.5.4.B9	L242A	the mutation causes a decrease of the enzyme activity	722114	
3.5.4.B9	L242K	the mutation causes a decrease of the enzyme activity	722114	
3.5.4.B9	additional information	CD2-2, possessing the deamination activity, incorporated efficiently into HIV-1 is unable to mutate viral cDNA. Construction of three A3G mutants CD1-1, CD2-2 and CD2-1, which contain duplicate CD1 domain, duplicate CD2 domain, and position switched CD domain, respectively. The two CD domains are functionally equivalent in virion encapsidation and the interaction with HIV-1 Vif of hA3G, whereas CD domain switch or replacement greatly affect the sensitivity to Vif-induced degradation, editing and antiviral activity of hA3G. The switch of the CD domain affects nucleotide sequence preference pattern of the deaminase. The mutants show a nucleotide sequence preference pattern	721103	
3.5.4.B9	additional information	comparison of Apo3G native and monomeric N-mutant F/W ssDNA substrate binding and catalysis, overview	712428	
3.5.4.B9	additional information	phospho-mimetic mutations inhibit DNA cytidine deaminase activity	719945	
3.5.4.B9	N244A	the mutant shows no deamination activity	723261	
3.5.4.B9	P210A	1.4% of wild-type activity	754123	
3.5.4.B9	P210A	1.4% of wild-type activtiy	754123	
3.5.4.B9	P210A	the variant has 1% of the catalytic efficiency of the wild type protein	734319	
3.5.4.B9	P210G	9.9% of wild-type activity	754123	
3.5.4.B9	P210G	9.9% of wild-type activtiy	754123	
3.5.4.B9	P210G	the variant has 10% of the catalytic efficiency of the wild type protein	734319	
3.5.4.B9	Q245A	5.5% of wild-type activity	754123	
3.5.4.B9	Q245A	5.5% of wild-type activtiy	754123	
3.5.4.B9	Q245A	the mutation nearly abolishes the catalytic efficiency to 5% compared to the wild type protein	734319	
3.5.4.B9	Q380A	68.5% of wild-type activity	754123	
3.5.4.B9	Q380A	68.5% of wild-type activtiy	754123	
3.5.4.B9	Q380A	the variant has 68% of the catalytic efficiency of the wild type protein	734319	
3.5.4.B9	R213E	the mutant shows about 3% deamination activity compared to the wild type enzyme	723261	
3.5.4.B9	R215E	the mutant shows no deamination activity	723261	
3.5.4.B9	R256A	1.3% of wild-type activity	754123	
3.5.4.B9	R256A	1.3% of wild-type activtiy	754123	
3.5.4.B9	R256A	the mutation nearly abolishes the catalytic efficiency to 1% compared to the wild type protein	734319	
3.5.4.B9	R256E	the mutant shows about 3% deamination activity compared to the wild type enzyme	723261	
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	712428	
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	723261	
3.5.4.B9	R374A	3.4% of wild-type activity	754123	
3.5.4.B9	R374A	3.4% of wild-type activtiy	754123	
3.5.4.B9	R374A	the variant has 3% of the catalytic efficiency of the wild type protein	734319	
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	723261	
3.5.4.B9	R376A	14.9% of wild-type activity	754123	
3.5.4.B9	R376A	14.9% of wild-type activtiy	754123	
3.5.4.B9	R376A	the variant has 15% of the catalytic efficiency of the wild type protein	734319	
3.5.4.B9	T203A	the mutation causes a decrease of the enzyme activity	722114	
3.5.4.B9	T218A	site-directed mutagenesis	719945	
3.5.4.B9	T218E	site-directed mutagenesis	719945	
3.5.4.B9	T27A	site-directed mutagenesis	719945	
3.5.4.B9	T27E	site-directed mutagenesis	719945	
3.5.4.B9	V233A	the mutation causes a decrease of the enzyme activity	722114	
3.5.4.B9	V233K	the mutation causes a decrease of the enzyme activity	722114	
3.5.4.B9	W232A	the mutation causes a decrease of the enzyme activity	722114	
3.5.4.B9	W285A	the mutant shows no deamination activity	723261	
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	712428	
3.5.4.B9	Y315A	the mutant shows no deamination activity	723261