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. 2011 Jun 13;108(26):10520–10525. doi: 10.1073/pnas.1104989108

Table 1.

Kinetic parameters for ht-ADH variants at pH 7, 30 °C

Enzyme kcat, s-1 Km (Alcohol), mM Km (NAD+), mM Inline graphic*
Wild type 24.9 (±2.5) 6.8 (±0.5) 1.1 (±0.1) 3.2 (±0.2)
L176V 1.7 (±0.1) 5.3 (±0.9) 1.2 (±0.2) 4.1 (±0.4)
L176A 2.8 (±0.3) 5.8 (±1.5) 2.6 (±0.6) 4.1 (±0.6)
L176G 7.7 (±1.4) 9.8 (±3.4) 25 (±8) 4.0 (±1.1)
L176Δ 0.43 (±0.09) 7.5 (±3.5) 37 (±14) 4.3 (±1.3)
V260A 2.4 (±0.2) 4.2 (±0.8) 10 (±1.6) 4.1 (±0.7)

*This is the ratio of kcat measured with H-benzyl alcohol to that measured with D-benzyl alcohol.

The Arrhenius break for V260A is at approximately 40 °C; the rest are at 30 °C.