Enolase: Difference between revisions
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===2, 3-diketo-5-methylthiopentyl-1-phosphate enolase=== | ===2, 3-diketo-5-methylthiopentyl-1-phosphate enolase=== | ||
[[ | [[2zvi]] – DK-MTP-1-P ENO – ''Bacillus subtilis''<br /> | ||
[[2oej]] - BkDK-MTP-1-P ENO + Pi – ''Geobacillus kaustophilus''<br /> | [[2oej]] - BkDK-MTP-1-P ENO + Pi – ''Geobacillus kaustophilus''<br /> | ||
[[2oek]], [[2oel]] - BkDK-MTP-1-P ENO + ion<br /> | [[2oek]], [[2oel]] - BkDK-MTP-1-P ENO + ion<br /> | ||
Revision as of 12:39, 14 June 2011
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| Yeast enolase complex with phosphoenolpyruvate and phosphoglycerate, 1one | |||||||||
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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 | ||||||||
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: it is a reversible dehydration reaction.[2]. Enolase is expressed abundantly in most cells and has been proven useful as a model to study mechanisms of enzyme action and structural analysis [3].
StructureStructure
The of enolase contains both alpha helices and beta sheets. The beta sheets are mainly parallel[4]. As shown in the figure, enolase has about 36 alpha helices and 22 beta sheets (18 alpha helices and 11 beta sheets per domain). Enolase consists of two domains.
Structural Clasification of Proteins (SCOP)[5]
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.
MechanismMechanism
The of enolase as shown, involves Lys 345, Lys 396, Glu 168, Glu 211, and His 159. Enolase forms a complex with two at its active site. The substrate, 2PG, binds to the two . The Mg 2+ then forms a bond at the deprotonated carboxylic acid on the 1'C to connect it with enolase. It also is connects to Glu 211 and Lys 345. Glu 211 makes a hydrogen bond with the alcohol group on the 3'C. Lys 345 deprotonates the 2'C and then the 2'C forms an alkene with the 1'C which then moves the electrons forming the ketone onto the oxygen making it have a negative charge. The other oxygen, which already has a negative charge, then moves its electron to form a ketone with the 1'C. The electrons that made up the alkene between the 1'C adn 2'C then moves to form an alkene between the 2'C and 3'C. This breaks the bond with the alcohol on the 3'C which deprotonates Glu 211 on enolase to form H2O. 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.[7]
KineticsKinetics
![V vs. [PGA]; PGA is 2PG, the top curve has [Mg2+] of 10^-3 M and the bottom curve has [Mg2+] of 106-2 M](/w/File:Enolase_kinetics.jpeg)
Since Mg2+ is essential for binding the substrate, 2-PG, it is also needed at a specific quality in order to have a good rate, or velocity. The graph shows the V vs. [PGA], in which PGA is 2-PG, with two different concentrations of Mg2+. The upper curve, which also has greater Vmax, has an Mg2+ concentration of 10^-3 M while the lower curve, which has a lower Vmax, has an Mg2+ concentration of 10^-2 M[9]. The Km is also larger the upper curve making the higher [Mg2+] more desirable.
RegulationRegulation
Enolase is found on the surface of a variety of eukaryotic cells as a strong plamingoen-binding receptor and on the surface of hematopietic celss such as monocytes, T cells and B cells, neuronal celss and endothelial cells. Enolase in muscle can bind other glycolytic enzymes, such as phosphoglycerate mutase, muscle creatine kinase, pyruvate kinase, and muscle troponin, with high affinity. This suggests that they make a functional glycolytic segment in the muscle where ATP production is required in order for the muscle to contract. Myc-binding protein (MBP-1) is similar to the a-enolse structure and is found in the nucleus as a DNA-binding protein[10]. Enolase is regulated by the concentration of Mg2+ and the previous steps of glycolysis.
3D structures of enolase3D structures of enolase
Update June 2011
EnolaseEnolase
3dip, 2qgy – ENO – unidentified
1oep - TbENO – Trypanosoma brucei
2ptw – TbENO (mutant)
2ptx - TbENO (mutant) + sulfate
2pty - TbENO (mutant) + PEP
2ptz, 2pu0, 2pu1 - TbENO (mutant) + PAH
2pa6 – ENO – Methanocaldococcus jannaschii
1w6t – ENO – Streptococcus pneumoniae
1iyx – ENO – Enterococcus hirae
1pdy, 1pdz – ENO – European lobster
3qn3 – ENO – Campylobacter jejuni
Enolase 1Enolase 1
3b97, 2psn – hENO1 - human
3otr – ENO1 – Toxoplasma gondii
1e9i - EcENO1 – Escherichia coli
2xgz, 2xh0, 2xh2, 2xh4, 2xh7 – EcENO1 residues 2-437 (mutant)
3h8a, 2fym – EcENO1 + RNase E
3enl, 4enl – yENO1 - yeast
2al1, 2al2, 1ebh – yENO1 + Mg
1p43, 1p48 – yENO1 (mutant)
1ebg, 1els - yENO1 + PAH
1l8p - yENO1 (mutant) + PAH
2one, 1one – yENO1 + PEP + phosphoglycerate
5enl, 7enl - yENO1 + phosphoglycerate
1nel, 6enl – yENO1 + inhibitor
Enolase 2Enolase 2
1te6 – hENO2
2akm, 2akz – hENO2 + inhibitor
Enolase 3Enolase 3
2xsx - hENO3
2, 3-diketo-5-methylthiopentyl-1-phosphate enolase2, 3-diketo-5-methylthiopentyl-1-phosphate enolase
2zvi – DK-MTP-1-P ENO – Bacillus subtilis
2oej - BkDK-MTP-1-P ENO + Pi – Geobacillus kaustophilus
2oek, 2oel - BkDK-MTP-1-P ENO + ion
2oem - BkDK-MTP-1-P ENO + Mg + phosphate derivative
Additional ResourcesAdditional Resources
For additional information, see: Carbohydrate Metabolism
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.
- ↑ Pancholi, V. "Multifunctional a-Enolase: Its Role in Diseases." CMLS, Cellular and Molecular Life Sciences 58 (2001): 902-20.
- ↑ 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.
- ↑ Westhead, E. W., and BO G. Malmstrom. "The Chemical Kinetics of the Enolase Reaction with Special References to the Use of Mixed Solvents." The Journal of Biological Chemistry 228 (1957): 655-71.
- ↑ Westhead, E. W., and BO G. Malmstrom. "The Chemical Kinetics of the Enolase Reaction with Special References to the Use of Mixed Solvents." The Journal of Biological Chemistry 228 (1957): 655-71.
- ↑ Pancholi, V. "Multifunctional a-Enolase: Its Role in Diseases." CMLS, Cellular and Molecular Life Sciences 58 (2001): 902-20.