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<StructureSection load='1one' size='450' side='right' caption='Yeast enolase dimer complex with phosphoenolpyruvate and phosphoglycerate, [[1one]]' scene='Enolase/Enolase/1'><scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> 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.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=487|}}</ref>  Enolase is used to convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis: it is a reversible dehydration reaction.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>.  Enolase is expressed abundantly in most cells and has been proven useful as a model to study mechanisms of enzyme action and structural analysis <ref>{{journal}}</ref>. As with the reaction below, Enolase must have a divalent metal cation present to activate or deactivate the enzyme. The best cofactor would be Mg2+, but many, including Zn2+, Mn2+ and Co2+ can be used. The metal ion works by binding to the enzyme at the active site and producing a conformational change. This makes it possible for the substrate (2-PGA) to bind at the Enolase active site. Once this happens, a second metal ion comes in and binds to the enzyme to activate the Enolase catalytic ability.  For sequence alignment see [[Enolase multiple sequence alignment]].
<StructureSection load='1one' size='350' side='right' caption='Yeast enolase dimer complex with phosphoenolpyruvate and phosphoglycerate, [[1one]]' scene='Enolase/Enolase/1'><scene name='Cory_Tiedeman_Sandbox_1/Enolase/1'>Enolase</scene> 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.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=487|}}</ref>  Enolase is used to convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in the 9th reaction of glycolysis: it is a reversible dehydration reaction.<ref>{{textbook |author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.|title=Fundamentals of Biochemistry: Life at the Molecular Level|edition= 3|pages=500|}}</ref>.  Enolase is expressed abundantly in most cells and has been proven useful as a model to study mechanisms of enzyme action and structural analysis <ref>{{journal}}</ref>. As with the reaction below, Enolase must have a divalent metal cation present to activate or deactivate the enzyme. The best cofactor would be Mg2+, but many, including Zn2+, Mn2+ and Co2+ can be used. The metal ion works by binding to the enzyme at the active site and producing a conformational change. This makes it possible for the substrate (2-PGA) to bind at the Enolase active site. Once this happens, a second metal ion comes in and binds to the enzyme to activate the enolase catalytic ability.  See [[Glycolysis Enzymes]].  For sequence alignment see [[Enolase multiple sequence alignment]].
*'''Enolase 2''' or '''gamma enolase''' is found in neurons.
*'''2,3-diketo-5-methylthiopentyl-1-phosphate enolase''' is part of the Met salvage pathway.


==Structure==
==Structure==
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==Mechanism==
==Mechanism==
[[Image:mechanism.png|left|400px|The mechanism of 2PG to PEP using enolase.]]<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 two   
<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 two   
<scene name='Cory_Tiedeman_Sandbox_1/Mg/3'>Mg 2+'s</scene> at its active site.   
<scene name='Cory_Tiedeman_Sandbox_1/Mg/3'>Mg 2+'s</scene> at its active site.   
The substrate, 2PG, binds to the two <scene name='Cory_Tiedeman_Sandbox_1/Mechanism/4'>Mg2+'s, Glu 211, and Lys 345</scene>.  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.   
The substrate, 2PG, binds to the two <scene name='Cory_Tiedeman_Sandbox_1/Mechanism/4'>Mg2+'s, Glu 211, and Lys 345</scene>.  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.   
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Enolase is present in all tissues and organisms with the ability to do glycolysis or fermentation. Recent studies have Enolase concentration samples in order to determine certain conditions and their severity. For instance, high concentrations of Enolase in cerebrospinal fluid (CSF) are more strongly associated with astrocytoma than other enzymes like aldolase, pyruvate kinase, and creatine kinase. High concentrations of Enolase in the CSF are also linked to the fastest rate of tumor growth and increased chances of heart attack or stroke.
Enolase is present in all tissues and organisms with the ability to do glycolysis or fermentation. Recent studies have Enolase concentration samples in order to determine certain conditions and their severity. For instance, high concentrations of Enolase in cerebrospinal fluid (CSF) are more strongly associated with astrocytoma than other enzymes like aldolase, pyruvate kinase, and creatine kinase. High concentrations of Enolase in the CSF are also linked to the fastest rate of tumor growth and increased chances of heart attack or stroke.
Enolase can be competitively inhibited by fluoride for the substrate 2-PGA. In drinking water with added fluorination, oral bacteria Enolase activity is inhibited without harmed humans. This works to prevent cavities.
Enolase can be competitively inhibited by fluoride for the substrate 2-PGA. In drinking water with added fluorination, oral bacteria Enolase activity is inhibited without harmed humans. This works to prevent cavities.
</StructureSection>


==3D structures of enolase==
==3D structures of enolase==
[[Enolase 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*Enolase
 
**[[3dip]], [[2qgy]] – ENO – unidentified<BR />
**[[1oep]] - TbENO – ''Trypanosoma brucei''<BR />
**[[2ptw]] – TbENO (mutant) <BR />
**[[2ptx]] - TbENO (mutant) + sulfate<BR />
**[[2pty]] - TbENO (mutant) + PEP<BR />
**[[2ptz]], [[2pu0]], [[2pu1]] - TbENO (mutant) + PAH<BR />
**[[2pa6]] – ENO – ''Methanocaldococcus jannaschii''<BR />
**[[1w6t]] – ENO – ''Streptococcus pneumoniae''<BR />
**[[1iyx]] – ENO – ''Enterococcus hirae''<BR />
**[[1pdy]], [[1pdz]] – ENO – European lobster<br />
**[[3qn3]] – ENO – ''Campylobacter jejuni''<br />
**[[3tqp]] – ENO – ''Coxiella burnetii''<br />
**[[3ugv]] – ENO – ''Alpha proteobacterium''<br />
**[[4a3r]] – BsENO – ''Bacillus subtilis''<br />
**[[4h1z]] – ENO – ''Rhizobium meliloti''<br />
**[[4jn7]], [[4jn8]] – ENO – ''Agrobacterium radiobacter''<br />
**[[3zlf]], [[3zlg]], [[3zlh]] - ENO (mutant) – ''Streptococcus pyogenes''<br />
**[[4g7f]] - ENO – ''Trypanosoma cruzi''<br />
**[[4gir]], [[4gis]] - ENO – ''Vibrio harveyi''<br />
 
*Enolase 1
 
**[[3b97]], [[2psn]] – hENO1 - human<BR />
**[[3otr]] – ENO1 – ''Toxoplasma gondii''<BR />
**[[3qtp]] – ENO1 – ''Entamoeba histolytica''<br />
**[[1e9i]] - EcENO1 – ''Escherichia coli''<BR />
**[[2xgz]], [[2xh0]], [[2xh2]], [[2xh4]], [[2xh7]] – EcENO1 residues 2-437 (mutant) <BR />
**[[3uj2]] – ENO1 – ''Anaerostipes caccae''<br />
**[[3h8a]], [[2fym]] – EcENO1 + RNase E<BR />
**[[3enl]], [[4enl]] – yENO1 - yeast<BR />
**[[2al1]], [[2al2]], [[1ebh]] – yENO1 + Mg<BR />
**[[1p43]], [[1p48]] – yENO1 (mutant) <BR />
**[[1ebg]], [[1els]] - yENO1 + PAH<BR />
**[[1l8p]] - yENO1 (mutant) + PAH<BR />
**[[2one]], [[1one]] – yENO1 + PEP + phosphoglycerate<BR />
**[[5enl]], [[7enl]] - yENO1 + phosphoglycerate<BR />
**[[1nel]], [[6enl]] – yENO1 + inhibitor


*Enolase 2
**[[4ewj]] – ENO2 – ''Streptococcus suis''
*Enolase 3
**[[2xsx]] - hENO3
*γ Enolase (neuron specific enolase)
**[[1te6]], [[3ucc]], [[3ucd]], [[3uje]], [[3ujf]], [[3ujr]], [[3ujs]] – hENOγ<BR />
**[[2akm]], [[2akz]] – hENOγ + inhibitor<br />
*2, 3-diketo-5-methylthiopentyl-1-phosphate enolase
**[[2zvi]] – DK-MTP-1-P BsENO <br />
**[[2oej]] - BkDK-MTP-1-P ENO + Pi – ''Geobacillus kaustophilus''<br />
**[[2oek]], [[2oel]] - BkDK-MTP-1-P ENO + ion<br />
**[[2oem]] - BkDK-MTP-1-P ENO + Mg + phosphate derivative
}}
==Additional Resources==
==Additional Resources==
For additional information, see: [[Carbohydrate Metabolism]]
For additional information, see: [[Carbohydrate Metabolism]]
<br />
<br />
</StructureSection>


==References==
==References==

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Cory Tiedeman, David Canner, Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman
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