Cory Tiedeman Sandbox 1

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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. Enolase forms a complex with
<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/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>
+
<scene name='Cory_Tiedeman_Sandbox_1/Mg/3'>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 18:52, 1 March 2010

PDB ID 1one

Drag the structure with the mouse to rotate
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]


Structure

The of enolase contains both alpha helices and beta sheets. The beta sheets are mainly parellel[3]. 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)[4]

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.[5]


References

  1. ↑ text book
  2. ↑ text book
  3. ↑ 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>.]
  4. ↑ 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>.]
  5. ↑ text book

Proteopedia Page Contributors and Editors (what is this?)

Cory Tiedeman, David Canner

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