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. Author manuscript; available in PMC: 2010 Dec 1.
Published in final edited form as: FEBS J. 2009 Oct 23;276(23):6928–6941. doi: 10.1111/j.1742-4658.2009.07389.x

Table 2.

Steady state kinetics data for transacetylation by wild type and Y190 mutants at 25°C and pH 7.0

Hamster NAT2 Ka (mM) Kb (mM) kcat (s−1) kcat/Ka (s−1mM−1) kcat/Kb (s−1mM−1)
PNPA/Anisidine
graphic file with name nihms158494t1.jpg
WTa 2.8 ± 0.4a 0.34 ± 0.04a 260 ± 20a 100 ± 20a 790 ± 120a
Y190F 7.8 ± 0.6 0.58 ± 0.04 288 ± 14 37 ± 4 496 ± 58
Y190I 10.1 ± 1.5 0.18 ± 0.03 85 ± 12 8.4 ± 2.4 483 ± 160
Y190A 7.4 ± 0.5 0.25 ± 0.02 28 ± 2 3.8 ± 0.6 114 ± 16

PNPA/PABA
graphic file with name nihms158494t2.jpg
WTa 10 ± 1a 0.23 ± 0.02a 620 ± 40 a 62 ± 9 a 2700 ± 400a
Y190F 7.7 ± 0.9 0.22 ± 0.01 393 ± 29 51 ± 10 1786 ± 214
Y190I 4.5 ± 0.7 0.08 ± 0.01 60 ± 4 13 ± 3 746 ± 146
Y190A 7.5 ± 0.5 0.11 ± 0.01 38 ± 2 5 ± 1 345 ± 46

PNPA/pABglu
graphic file with name nihms158494t3.jpg
WTa 1.5 ± 0.1a 1.7 ± 0.1a 120 ± 3a 86 ± 3a 70 ± 5a
Y190F 2.8 ± 0.2 2.5 ± 0.2 86 ± 3 30 ± 3 34 ± 4
Y190I 11 ± 1 2.7 ± 0.2 77 ± 4 7 ± 1 28 ± 4
Y190A 5.6 ± 0.6 6.2 ± 0.6 16 ± 1 2.8 ± 0.5 2.6 ± 0.4

AcCoA/PNA
graphic file with name nihms158494t4.jpg
WTa 0.037 ± 0.003a 0.77 ± 0.06a 0.60 ± 0.02a 16 ± 2a 0.78 ± 0.08a
Y190F 0.14 ± 0.03 0.48 ± 0.10 0.31 ± 0.03 2.23 ± 0.79 0.66 ± 0.21
Y190I 0.71 ± 0.18 1.51 ± 0.44 0.89 ± 0.15 1.26 ± 0.54 0.60 ± 0.27
Y190A 1.49 ± 0.8 2.92 ± 1.64 0.25 ± 0.11 0.17 ± 0.16 0.087 ± 0.086

AcCoA/PABA WTa 3.4 ± 0.3a 0.12± 0.01a 200 ± 1a 60 ± 6a 1700 ± 200a
Y190F 1.8 ± 0.2 0.14 ± 0.02 189 ± 17 106 ± 15 1360 ± 226
Y190I 1.9 ± 0.6 0.06 ± 0.01 58 ± 9 30 ± 13 974 ± 377
Y190A 2.7 ± 0.9 0.28 ± 0.10 8.14± 2.23 3± 1 29 ± 11
a

Values for the “wild type” protein are taken from previously published research articles: [27]