Sandbox Reserved 800
From Proteopedia
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| + | == Introduction == | ||
| + | Enolase is an enzyme found in glycolysis. In glycolysis enolase is responsible for catalyzing the reaction of 2-phosphoglycerate to phosphoenolpyruvate, or the reverse reaction depending on the concentration of the substrates. Enolase can be found in any organism or tissue that is able to perform glycolysis or fermentation. | ||
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| + | == PBD Data == | ||
PBD: 2AKZ | PBD: 2AKZ | ||
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This Enzyme is a Dimer | This Enzyme is a Dimer | ||
| - | Enzyme Reaction | + | Enzyme Reaction: |
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2-phospho-D-glycerate <--> phosphoenolpyruvate + H2O | 2-phospho-D-glycerate <--> phosphoenolpyruvate + H2O | ||
<Structure load='2akz' size='500' frame='true' align='right' caption='Enolase' scene='Insert optional scene name here' /> | <Structure load='2akz' size='500' frame='true' align='right' caption='Enolase' scene='Insert optional scene name here' /> | ||
| - | This is <scene name='56/563212/Rainbow_enolate/1'> | + | This is a <scene name='56/563212/Rainbow_enolate/2'>rainbow colored enolate</scene>. It shows the N terminus in blue and the C terminus in red. This is <scene name='56/563212/Enolate_side_chain_a/1'>enolate side chain A</scene> with the helixes and sheets represented in different colors. This scene shows the <scene name='56/563212/Hydrophobic_residues/1'>hydrophobic residues</scene> of Enolate. The hydrophobic residues are shown in grey, and are mostly found on the inside portion of the enzyme away from water, while the hydrophilic residues are found more out the outer edge allowing them to interact with the solvent. <scene name='56/563212/Hydrogen_bonding/1'>Hydrogen bonds</scene> are shown in purple while the beta-sheets are shown in yellow. The way that the hydrogen bonds are set up shows that the beta-sheets are parallel in nature, however, there are also anti-parallel beta-sheets at other portions of the enzyme. <scene name='56/563212/Solvent_water/1'>Water</scene> is shown in red, with the enzyme in a grey and the ligand is in green. The water is mostly located on the outer edge of the Enolate with some clustering in and around the ligand binding site (water is only shown covering one side chain). The <scene name='56/563212/Interactions_with_ligand/1'>ligand binding site</scene> is shown here. The ligand (Malate) is interacting with mostly polar residues. The hydrogen bonds form stabilize malate in the binding pocket. There are also some non-polar side chains that are not involved in hydrogen bonding, but are important in the shape and stability of the binding pocket. The <scene name='56/563212/Catalytic_residues/2'>catalytic residues</scene> are shown here in white. They interact with the non-hydrolysable substrate in the active site. |
Current revision
| This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807. |
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Introduction
Enolase is an enzyme found in glycolysis. In glycolysis enolase is responsible for catalyzing the reaction of 2-phosphoglycerate to phosphoenolpyruvate, or the reverse reaction depending on the concentration of the substrates. Enolase can be found in any organism or tissue that is able to perform glycolysis or fermentation.
PBD Data
PBD: 2AKZ
Catalytic Residus: E 166; H 189; E 209; V 240; K 342; H 370; A 393;
Ligands: G37; A38; S39; T40; I42; H157; Q165; E166; E209; S248; E249; Q297; K342; R371; S372
Metal Ligand Binding Sites: S39; Q165; E166; D244; E242 D317; L340 K342; K393
This Enzyme is a Dimer
Enzyme Reaction:
2-phospho-D-glycerate <--> phosphoenolpyruvate + H2O
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This is a . It shows the N terminus in blue and the C terminus in red. This is with the helixes and sheets represented in different colors. This scene shows the of Enolate. The hydrophobic residues are shown in grey, and are mostly found on the inside portion of the enzyme away from water, while the hydrophilic residues are found more out the outer edge allowing them to interact with the solvent. are shown in purple while the beta-sheets are shown in yellow. The way that the hydrogen bonds are set up shows that the beta-sheets are parallel in nature, however, there are also anti-parallel beta-sheets at other portions of the enzyme. is shown in red, with the enzyme in a grey and the ligand is in green. The water is mostly located on the outer edge of the Enolate with some clustering in and around the ligand binding site (water is only shown covering one side chain). The is shown here. The ligand (Malate) is interacting with mostly polar residues. The hydrogen bonds form stabilize malate in the binding pocket. There are also some non-polar side chains that are not involved in hydrogen bonding, but are important in the shape and stability of the binding pocket. The are shown here in white. They interact with the non-hydrolysable substrate in the active site.
