4. In enolase, replacement of the catalytically active K345 by the unusual amino

Q: 4. In enolase, replacement of the catalytically active K345 by the unusual amino

a. The shown amino acid is lysine and its primary role is to donate the proton. the side chain of lysine contains proton donor acceptor group i.e, NH3+ b. If one replaces lysine with aspartate or glutamate which is also proton donor groups, it would decreases the activity of enzyme enolase. this is due to the presence of negative charge on aspartate or glutamate after removing proton charge difference decrease activity. b.

ID: 262310 • Letter: 4

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4. In enolase, replacement of the catalytically active K345 by the unusual amino acid shown below leads to a 1000-fold decrease in the catalytic rate. a) What is the chemical role of K345? b) Given that this unusual amino acid can carry out the same chemistry as that of K345, then what might account for this difference in activity? (Hint: the pKa difference between this amino acid side chain and that of K would NOT be significant enough to account for this decrease, e.g. see the small difference in the pKas of the side chains of D versus E.) H3N NH3

Explanation / Answer

The shown amino acid is lysine and its primary role is to donate the proton. the side chain of lysine contains proton donor acceptor group i.e, NH3+

If one replaces lysine with aspartate or glutamate which is also proton donor groups, it would decreases the activity of enzyme enolase. this is due to the presence of negative charge on aspartate or glutamate after removing proton charge difference decrease activity.

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4. In enolase, replacement of the catalytically active K345 by the unusual amino

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