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. Author manuscript; available in PMC: 2018 Dec 27.
Published in final edited form as: J Am Chem Soc. 2017 Dec 15;139(51):18409–18427. doi: 10.1021/jacs.7b08418

Figure 10.

Figure 10

Impact of mutation at V260 in ht-ADH.74 Panel (a) displays a focused view of active-site hydrophobic side chains (Leu176 and Val260) that sit behind the nicotinamide ring of cofactor. Upon mutation of V260 to alanine (b), the break in kinetic at 30 °C in the WT ht-ADH is enhanced and the active site has been rigidified, as illustrated by the reversal of the temperature dependence of the KIE, above and below 30°C from that of WT (Figure 9a).