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. Author manuscript; available in PMC: 2010 Jun 9.
Published in final edited form as: Biochemistry. 2009 Jun 9;48(22):4959–4971. doi: 10.1021/bi900432n

Table 3.

pH Dependence for β-LS Dyad Mutantsa

kcat kcat/Km


β-LS pKa pKa pKb
WTb 8.07 ± 0.05 9.15 ± 0.06 7.95 ± 0.08
Y348F 8.37 ± 0.03 7.25 ± 0.05
Y348A
E382D 8.27 ± 0.08 9.5 ± 0.1 8.3 ± 0.2
a

(–) indicates no transition observed in the pH–rate profile from no detectable activity below pH 8.3. WT represents wild-type β-LS. Italic type shows the pK values that were further calculated from the observed pH–(kcat/Km) and reflects reverse protonation of the protein.

b

pKa in the wild-type pH–kcat profile previously reported in ref 11.