Chemistry, 12.09.2019 21:20, Teedollasign
Activity of the bacterial enzyme acetoacetate decarboxylase sharply declines below ph 6, suggesting there is an ionizable catalytic residue with pka ~ 6. using mutagenesis, this critical catalytic residue was determined to be lys-115. a) what is the typical pka of a lysine side chain and what ratio of deprotonated to protonated lysine would be expected at ph 7.5 (standard ph inside a bacterium)
Answers: 1
![pH=pka+log\frac{[A^{-} ]}{[HA]}](/tpl/images/0229/1595/fae8c.png)
![7.5=10.5+log\frac{[A^{-} ]}{[HA]}\\-3.0=log\frac{[A^{-} ]}{[HA]}\\10^{-3.0}=\frac{[A^{-} ]}{[HA]}\\0.001=\frac{[A^{-} ]}{[HA]}](/tpl/images/0229/1595/47589.png)
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Activity of the bacterial enzyme acetoacetate decarboxylase sharply declines below ph 6, suggesting...
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