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. Author manuscript; available in PMC: 2011 Feb 1.
Published in final edited form as: Bioorg Med Chem Lett. 2010 Jan 4;20(3):841. doi: 10.1016/j.bmcl.2009.12.097

Table 1.

Substrate specificities of wild type DmdNK

substrate (100 µM) specific activity (µM min−1 mg−1)
THY * 60,000 ± 1010
fTHY (1) * 25,511 ± 455 (43%)
dC * 43,734 ± 660
fdC (2) 56,034 ± 1050 (128%)
ddT 1310 ± 87
fddT (3) 397 ± 36 (30%)
ddC 2005 ± 148
fddC (5) 52 ± 9 (2.6%)
FT 1189 ± 17
fFT (7) 144 ± 27 (12%)
AZT 1054 ± 14
fAZT (6) 128 ± 7 (12%)
d4T 70 ± 15
fd4T (4) 232 ± 20 (330%)

Specific activities were measured by spectrophotometric coupled-enzyme assay with 100 µM substrate and 1 mM ATP except for substrates marked with an asterisk (measured at 10 µM substrate concentration under vmax conditions). Experiments were performed in triplicates. Percentage in parentheses is relative activity of fluorescent analog over non-fluorescent analog.