Skip to main content
. Author manuscript; available in PMC: 2010 Nov 1.
Published in final edited form as: Chimia (Aarau). 2009 Nov 1;63(11):737–744. doi: 10.2533/chimia.2009.737

Table 3.

Catalytic performance of ddT-kinases

WT DmdNK R4.V3 R4.V3-[85] R4.V3-[172]
Thr85Met … Glu172Val Thr85Met …
Glu172Val Tyr179Phe Tyr179Phe
Tyr179Phe His193Tyr His193Tyr
His193Tyr
T 4813 0.1 (−48,000) 1.4 (−3,400) 326 (−14)
dC 5850 0.36 (−16,000) 0.39 (−15,000) 2925 (−2)
dA 161 nd nd 57 (−2.5)
dG 28 nd nd 6 (−4.5)
ddT 4.6 3 (−1.5) 28 (+6) 2.6 (−1.8)
fddT 1.3 1.9 (+1.5) 0.4 (−3) 7.5 (+6)

The kcat/KM values (× 103 s−1 M−1) of the parental enzyme, as well as evolved variants are listed. The fold change relative to DmdNK are shown in parentheses. nd = not detectable. Data were adapted from ref. [42].