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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 1:

Kinetic parameters of mTrxR enzymes with Trx as substrate.

Enzyme kcat (min−1) KM (μM) kcat/KM (min−1 M−1) kcat/KM(mutant)
/kcat/KM(WT)
mTrxR-CUG 1770 ± 60 42 ± 4.4 4.2 x107
mTrxR-C(αMe)UG 15 ± 0.76 26 ± 4.8 5.8 x105 0.0138
mTrxRΔ3 a NA NA NA
a

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