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. 2016 Oct 11;6:34993. doi: 10.1038/srep34993

Table 2. Kinetic constants of TyrBm on its natural substrates and HQ.

Substrate Km (mM) Vmax (μmole min−1 mg−1) kcat (s−1) kcat/Km (s−1 mM−1)
L-tyrosine 0.082 ± 0.006 3.62 ± 0.06 2.1 25.6
L-dopa 0.24 ± 0.02 30.3 ± 0.6 17.8 74.2
HQ 0.27 ± 0.05 19 ± 1 11.3 41.9

Data was extracted from Figs 1, 2 and Supplementary Fig. S1. Each value represents the mean ± SD of five independent experiments.