Cory Tiedeman Sandbox 1
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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. Enolase is used to convert2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis.
StructureStructure
The of enolase contains both alpha helices and beta sheets. The beta sheets are mainly parellel[1]. As shown in the figure, enolase has about 36 alpha helixes and 22 beta sheets (18 alpha helices and 11 beta sheets per domain).
Structural Clasification of Proteins (SCOP)[2]
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)
MechanismMechanism
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. As the mechanism shows, bonds then get moved around to create a different ketone and to remove an alcohol and form an alkene. Then the new molecule is released from enolase as PEP. PEP then goes on through another step in glycolysis to create pyruvate.
Fluoride ions inhibits glcolysis by forming a bond with Mg 2+ thus blocks the substrate (2PG) from binding to the active site of enolase.
ReferencesReferences
- ↑ The scop authors. Structural Classification of Proteins. “Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae). 2009. 2/26 2010. [<http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html>.]
- ↑ The scop authors. Structural Classification of Proteins. “Protein: Enolase from Baker's yeast (Saccharomyces cerevisiae). 2009. 2/26 2010. [<http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.b.bc.b.b.html>.]