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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 2:

Kinetic parameters of mTrxR enzymes with H2O2 as substrate.

Enzyme kcat (min−1) KM (μM) kcat/KM (min−1 M−1) kcat/KM(mutant)
/kcat/KM(WT)
mTrxR-CUG 1110 ± 62 134 ± 16 8.2 x103
mTrxR-C(αMe)UG 10.5 ± 0.5 35 ± 8.0 3.0 x102 0.037
mTrxRΔ3 a NA NA NA
a

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