Cory Tiedeman Sandbox 1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 23: | Line 23: | ||
==Mechanism== | ==Mechanism== | ||
The | The | ||
<scene name='Cory_Tiedeman_Sandbox_1/Active_sice/1'>active site</scene> of enolase as shown, involves Lys 345, Lys 396, Glu 168, Glu 211, and His 159. | <scene name='Cory_Tiedeman_Sandbox_1/Active_sice/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/Mg/ | <scene name='Cory_Tiedeman_Sandbox_1/Mg/2'>Mg 2+</scene> 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.<ref>{{text book |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref> | ||
==References== | ==References== | ||
{{Reflist}} | {{Reflist}} | ||
Revision as of 08:06, 1 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 | ||||||||
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]
StructureStructure
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)
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. 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]