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. Author manuscript; available in PMC: 2021 Jul 6.
Published in final edited form as: J Am Chem Soc. 2019 Aug 5;141(32):12634–12647. doi: 10.1021/jacs.9b04470

Table 1.

Enzyme kinetics data for WT and acid-loop alanine scanning mutants.1

k2 (s−1) k3(s−1) kcat/KM (s−1mM−1)2 Km (mM)2 Apo loop3
WT 270 ± 60 28 ± 7 100 ± 10 0.57 ± 0.08 open
T177A 270 ± 30 38 ± 8 100 ± 20 0.35 ± 0.08 closed
P180A 250 ± 10 25 ± 2 230 ± 50 0.39 ± 0.05 closed
F182A 32 ± 2 1.3 ± 0.1 30 ± 50 0.11 ± 0.09 open/closed
P185A 58 ± 3 5.0 ± 0.1 13 ± 2 2.5 ± 0.3 open
P188A 133 ± 32 47 ± 10 230 ± 40 0.42 ± 0.07 open/closed
1

All pre-steady state kinetics was performed at 3.5°C, at a pH of 5.4.

2

Data was previously collected from Cui et al. 2017 at 25°C.31

3

Loop conformation based on NMR and X-ray crystallographic studies.