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Results 1 - 6 of 6
EC Number
Subunits
Commentary
Reference
monomer or dimer
x * 46000, the enzyme is active in monomeric, dimeric, and larger oligomeric states
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A3G contains two cytidine deaminase domains. The CD2 domain possesses the deamination activity
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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
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APOBEC3G cytidine deaminase catalytically inactive N-terminal CD1 domain has a predicted large net positive charge, in contrast to the catalytically active CD2 domain, and is likely to govern the mobility of APOBEC3G cytidine deaminase on ssDNA, which should depend on metal ion concentration
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the enzyme is a mix of monomers, dimers, and higher order oligomers
Results 1 - 6 of 6