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. Author manuscript; available in PMC: 2020 Sep 23.
Published in final edited form as: Biochemistry. 2020 Aug 30;59(36):3300–3315. doi: 10.1021/acs.biochem.0c00608

Table 3:

Kinetic parameters of mTrxR enzymes with DTNB as substrate.

Enzyme kcat (min−1) KM (μM) kcat/KM (min−1 M−1) kcat/KM(mutant)
/kcat/KM(WT)
mTrxR-CUG 3170 ± 450 3 ± 0.7 1.1 x109 –
mTrxR-C(αMe)UG 1125 ± 145 5 ± 0.9 2.3 x108 0.209
mTrxRΔ3 a 2900 ± 500 12 ± 2.7 2.4 x108 0.218
a

The truncated enzyme ends at glycine 487 and is missing the C-terminal tripeptide.