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. Author manuscript; available in PMC: 2023 May 19.
Published in final edited form as: Methods Enzymol. 2020 Apr 20;641:373–399. doi: 10.1016/bs.mie.2020.03.009

Table 2.

Kinetic parameters of various nucleobase substrates.

Compound Km, μM kcata (×10−3) s−1 kcat/Kma (×10−3) s−1 μM−1 Ref.
Guanine 2.2 61a 28 a Hoops et al. (1995)
graphic file with name nihms-1861747-t0001.jpg
−CH2NH2 (preQ1) 0.39 45a 115a Hoops et al. (1995)
−CN (preQ0) 2.35 72a 31 a Hoops et al. (1995)
−CH2OH 23.0 45a 2.0a Hoops et al. (1995)
−H 172 45a 0.3a Hoops et al. (1995)
−CH3 255 45a 0.2a Hoops et al. (1995)
−CH2OCH3 57 47a 0.8a Hoops et al. (1995)
−CH2N(CH3)2 75 43a 0.6a Hoops et al. (1995)
−CONH2 26 69a 2.7a Hoops et al. (1995)
−CO2CH3 87 73a 0.8a Hoops et al. (1995)
−COCH3 26 73a 2.8a Hoops et al. (1995)
−CHO 22 73a 3.3a Hoops et al. (1995)
−CO2H 126 21a 0.2a Hoops et al. (1995)
−(PEG)3-thiazole orange 9.8 1.6 0.2 Alexander et al. (2015)
−C6H12-thiazole orange derivative 1.6 26.7 16.7 Zhou et al. (2017)
a

kcat were calculated from reported Vmax values using the reported enzyme concentration (50 nM), and reaction volume (400 μL) (Hoops et al., 1995).