Question

In: Chemistry

DIPF and Sarin and "organophosphate" insecticides are all irreversible inhibitors of enzymes with a "special" --...

DIPF and Sarin and "organophosphate" insecticides are all irreversible inhibitors of enzymes with a "special" -- highly reactive -- active-site Ser residue. Which of the following is true about DIPF (or Sarin or organophosphate insecticides)?

A.) DIPF forms a covalent phosphoester bond to the side chain of a Ser residue in enzymes that DIPF inhibits.
B.) DIPF (or Sarin or organophosphate insecticides) cannot kill humans (or any vertebrate).
C.) DIPF inhibition is reversible. Hence, an EI complex is analogous to an ES complex.
D.)After DIPF reacts with an enzyme (to inhibit it) the phosphate part of DIPF is released and the rest of the molecule, including F, remains attached to the enzyme.
E.) none of the above is a true statement.

Solutions

Expert Solution

A.) DIPF forms a covalent phosphoester bond to the side chain of a Ser residue in enzymes that DIPF inhibits. True
B.) DIPF (or Sarin or organophosphate insecticides) cannot kill humans (or any vertebrate) False
C.) DIPF inhibition is reversible. Hence, an EI complex is analogous to an ES complex. False

D.)After DIPF reacts with an enzyme (to inhibit it) the phosphate part of DIPF is released and the rest of the molecule, including F, remains attached to the enzyme. False

phosphoester bond is formed to the side chain of a Ser residue in enzymes.

  • Use of DIPF as enzyme inhibitor based on discovery that organophosphorous compounds, such as DIPF, acts as potent nerve poisons.DIPF is closely related chemically to nerve gas, whose lethality is due to the inactivation of acetylcholinesterase, an enzyme critical for the transmission of nerve impulses. Acetylcholinesterase cleaves the neurotransmitter acetylcholine, an essential step in normal functioning of nervous system.
  • Organophosphorus compounds, such as diisopropylphosphofluoridate, DIPF, are potent irreversible inhibitors of enzymes that have active seryl residues at their catalytic sites.

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