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. Author manuscript; available in PMC: 2016 Jul 22.
Published in final edited form as: FEBS Lett. 2015 Jul 2;589(16):2124–2130. doi: 10.1016/j.febslet.2015.06.028

Table 1.

Single turnover kinetic analysis of 3′-5′ addition catalyzed by TLPs

kobs (min−1) First Additiona kobs (min−1) Complete extensiona
Enzyme U+3-start C+4-start U+3-start C+4-start
AcaTLP1 0.022 ± 0.001 2.6 ± 0.3 0.018 ± 0.011 1.6 ± 0.4
AcaTLP2 1.2 ± 0.2 11 ± 4 0.79 ± 0.32 4.9 ± 2.2
DdiTLP3 0.0084 ± 0.0004b 0.52 ± 0.18 0.0094 ± 0.0014b 0.60 ± 0.21
DdiTLP4 0.0076 ± 0.0014b 0.98 ± 0.27 0.0074 ± 0.0024b 0.71 ± 0.05
a

Average of three independent measurements performed under saturating conditions with respect to enzyme, ATP and added NTP; errors are standard deviations.

b

Rates were calculated by the method of linear initial rates because of slow reaction rates.