Cory Tiedeman Sandbox 1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 15: | Line 15: | ||
==Mechanism== | ==Mechanism== | ||
[[Image:mechanism.png|left|400px]] | [[Image:mechanism.png|left|400px]]<ref>{{website2}}</ref> | ||
The | The | ||
<scene name='Cory_Tiedeman_Sandbox_1/Active_site/1'>active site</scene> of enolase as shown, involves Lys 345, Lys 396, Glu 168, Glu 211, and His 159. Enolase forms a complex with | <scene name='Cory_Tiedeman_Sandbox_1/Active_site/1'>active site</scene> of enolase as shown, involves Lys 345, Lys 396, Glu 168, Glu 211, and His 159. Enolase forms a complex with | ||
Revision as of 16:03, 19 March 2010
| |||||||||
| 1one, resolution 1.80Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||||
| Non-Standard Residues: | |||||||||
| Activity: | Phosphopyruvate hydratase, with EC number 4.2.1.11 | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
is an enzyme that catalyzes a reaction of glycolysis. Glycolysis converts glucose into two 3-carbon molecules called pyruvate. The energy released during glycolysis is used to make ATP.[1] Enolase is used to convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis.[2]
StructureStructure
The of enolase contains both alpha helices and beta sheets. The beta sheets are mainly parallel[3]. As shown in the figure, enolase has about 36 alpha helices and 22 beta sheets (18 alpha helices and 11 beta sheets per domain).
Structural Clasification of Proteins (SCOP)[4]
Enolase is in the alpha and beta proteins class and has a fold of TIM beta/alpha-barrel. It comes from the Superfamily on Enolase C-terminal domain-like and is in the enolase family. This specific enolase is found in the species: Saccharomyces cerevisiae, which is baker's yeast.
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 glycolysis by forming a bond with Mg 2+ thus blocks the substrate (2PG) from binding to the active site of enolase.[6]
KineticsKinetics
ReferencesReferences
- ↑ Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry: Life at the Molecular Level. 3rd ed. Hoboken, NJ: John Wiley & Sons, Inc., 2008.
- ↑ Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry: Life at the Molecular Level. 3rd ed. Hoboken, NJ: John Wiley & Sons, Inc., 2008.
- ↑ 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>.]
- ↑ Nguyen, Tram, and Katelyn Thompson. "Mechanism of Enolase Converting 2-Phosphoglycerate to Phosphoenolpyruvate." ChemDraw 10.0: Public Domain, 2008. [1].
- ↑ Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry: Life at the Molecular Level. 3rd ed. Hoboken, NJ: John Wiley & Sons, Inc., 2008.