Cory Tiedeman Sandbox 1
From Proteopedia
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| 1one, resolution 1.80Å () | |||||||||
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| Ligands: | , | ||||||||
| Non-Standard Residues: | |||||||||
| Activity: | Phosphopyruvate hydratase, with EC number 4.2.1.11 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Enolase is an enzyme that catalyzes a reaction of glycolysis. Glycolysis converts glucose into two 3-carbon molecules called pyrubate. The energy released during glycolysis is used to make ATP.[1] Enolase is used to convert2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis.[2]
Structure
Structural Clasification of Proteins (SCOP)
Class: alpha and beta proteins (a/b)
Fold: TIM beta/alpha-barrel
Superfamily: Enolase C-terminal domain-like
Family: Enolase
Species: Baker's yeast (Saccharomyces cerevisiae)
Mechanism
The of enolase as shown, involves Lys 345, Lys 396, Glu 168, Glu 211, and His 159. Enolase forms a complex with at its active site. The Mg 2+ then forms a bond with 2PG to connect it with enolase. Fluoride ions inhibits glcolysis by forming a bond with Mg 2+ thus blocks the substrate (2PG) from binding to the active site of enolase.[3]
