phosphopyruvate hydratase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O. [EC:4.2.1.11, ISBN:0198506732]

Phosphopyruvate hydratase, also known as enolase, catalyzes the reversible dehydration of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP). This reaction is a key step in glycolysis, the central pathway for glucose metabolism.

Enolase is a metalloenzyme that requires divalent metal ions, typically Mg2+ or Mn2+, for activity. The mechanism of the reaction involves the following steps:

1. **Binding of 2-PG:** The substrate, 2-PG, binds to the active site of enolase.
2. **Dehydration:** The enzyme removes a water molecule from 2-PG, forming a carbon-carbon double bond and generating PEP.
3. **Release of PEP:** The product, PEP, is released from the enzyme.

The active site of enolase contains a number of amino acid residues that are essential for catalysis. These residues include:

* **Lysine:** Lysine residues play a role in stabilizing the transition state and promoting the removal of water.
* **Glutamic acid:** Glutamic acid residues are involved in the proton transfer steps of the reaction.
* **Metal ion:** The metal ion, Mg2+, coordinates with the phosphate group of 2-PG and facilitates the dehydration reaction.

The activity of enolase is tightly regulated in cells, ensuring that the flux through glycolysis is balanced with the needs of the cell. Enolase is also a target for some antimicrobial drugs, which inhibit its activity and disrupt the metabolism of pathogens.
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Proteins (4)

Compounds (2)