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. Author manuscript; available in PMC: 2014 Sep 24.
Published in final edited form as: Biochemistry. 2013 Sep 11;52(38):6724–6736. doi: 10.1021/bi400665t

Table 1.

LigAB Steady-State Kinetic Parameters Measured with PCA and Analogous Substrates in Air-Saturated Buffer

substrate Kmapp (μM) kcatapp (s−1) kcatappKmapp (M−1 s−1) partition ratioa jinactapp (s−1)
PCA 51 ± 4 216 ± 3 4.26 × 106 ~18000 0.012c
gallate 441 ± 55 53 ± 2 1.21 × 105 ~2500 0.021b
3OMG 2319 ± 316 7.3 ± 0.5 3.13 × 103 ~5600 0.0013c
DHBAm 3263 ± 327 104 ± 5 3.20 × 104 ~3200 0.033d
a

Estimated from the jinactapp and kcatapp (eq 5).

b

Calculated from a fit of eq 4 to js values determined from the fitting of progress curves (eq 3) at different concentrations of gallate.

c

Concentration dependent inactivation was not observed for PCA or 3OMG. jinactapp was calculated as an average of the js values determined from the fitting of eq 3 to progress curves at different substrate concentrations.

d

Concentration dependent inactivation was observed for DHBAm; however, the behavior is inconsistent with eq 4 due to highly inactivating product inhibition. jinactapp was calculated from an average of the js values determined from the fitting of eq 3 to progress curves of reactions with 1000–5000 μM DHBAm.