Skip to main content
. Author manuscript; available in PMC: 2013 May 20.
Published in final edited form as: Biochemistry. 2011 Jun 10;50(26):5870–5882. doi: 10.1021/bi200107n

Table 3.

The kinetic parameters of wild-type SmTGR and Sec597Cys reacting with the substrates, DTNB (DTNB activity), GSSG (GR activity), and Trx (TrxR activity)

DTNB activity (kcat, s−1) % of WT Km for DTNB (μM)
WT 16 ± 0.6 - 319 ± 47
Sec597Cys 4 ± 0.1 25a, 6.8b 107 ± 10
GR activity (kcat, s−1) % of WT Km for GSSG (μM)
WT 19 ± 1.2 - 42 ± 6
Sec597Cys 4 ± 0.6 21a, 5.7b 71 ± 24
TrxR activity (kcat, s−1) % of WT Km for Trx (μM)
WT 19 ± 1 - 8 ± 0.3
Sec597Cys 3.5 ± 0.1 18a, 4.9b 15 ± 2.3
a

inhibition is determined by the activities of Sec597Cys compared to those of wild-type enzyme

b

inhibition is determined by the activities of Sec597Cys compared to those of wild-type enzyme when it is considered that only 27 % of wild-type enzyme is full length whereas 100 % of Sec597Cys is full length