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Results 1 - 6 of 6
EC Number Subunits Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.B9dimer - 721668, 723256
Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.B9monomer or dimer x * 46000, the enzyme is active in monomeric, dimeric, and larger oligomeric states 722665
Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.B9More A3G contains two cytidine deaminase domains. The CD2 domain possesses the deamination activity 721103
Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.B9More 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 712428
Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.B9More 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 720014
Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.B9More the enzyme is a mix of monomers, dimers, and higher order oligomers 721999
Results 1 - 6 of 6