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. 2021 Jan 18;14(1):74. doi: 10.3390/ph14010074

Table 2.

Inhibition type, mechanism, and the inhibition constant values of the examined compounds on the diphenolase activity of mushroom tyrosinase.

Compound Inhibition Mechanism Inhibition Type Ki 1 ± Standard Error (µM)
(n = 3)
Kis 2 ± Standard Error (µM)
(n = 3)
TSC 1 reversible mixed 5.0 ± 1.4 27.5 ± 3.5
TSC 2 reversible mixed 1.0 ± 0.1 9.7 ± 3.1
TSC 3 reversible competitive 0.6 ± 0.01 -
TSC 4 reversible mixed 8.0 ± 0.9 30.4 ± 0.5
TSC 5 reversible mixed 0.6 ± 0.1 3.05 ± 1.1
TSC 6 reversible competitive 0.2 ± 0.06 3.5 ± 0.8
TSC 7 reversible mixed 0.7 ± 0.1 5.3 ± 2.1
TSC 8 reversible mixed 0.6 ± 0.08 5.4 ± 0.1
TSC 9 reversible competitive 0.6 ± 0.06 -
TSC 10 reversible mixed 8.6 ± 0.5 43.3 ± 3.0
TSC 11 reversible competitive 0.4 ± 0.02 -
TSC 12 reversible mixed 5.0 ± 1.4 27.5 ± 3.5
Kojic acid reversible mixed 26 ± 1 72 ± 3

1 Inhibition constant for enzyme–inhibitor complex; 2 inhibition constant for substrate–enzyme–inhibitor complex.