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Results 1 - 10 of 54 > >>
EC Number
Amino acid exchange
Commentary
Reference
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%
C288A/C291A
the mutant enzyme shows about 18% activity compared to the wild type enzyme
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%
C97A/C100A
the mutant enzyme shows about 18% activity compared to the wild type enzyme
D264A
the variant has 5% of the catalytic efficiency of the wild type protein
D316R/D317R
the mutant shows about 180% deamination activity and about 200% single-stranded DNA binding compared to the wild type enzyme
D316R/D317R
the mutations increase affinity for substrate and deamination specificity
D370A
the variant has 16% of the catalytic efficiency of the wild type protein
E259Q
site-directed mutagenesis
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
Results 1 - 10 of 54 > >>