Sandbox Reserved 807
From Proteopedia
| Line 4: | Line 4: | ||
==Introduction== | ==Introduction== | ||
| - | Enolase is an important enzyme for all cells. It is used in glycolysis to catalyze the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PEP) in the 9th reaction in glycolysis. This reaction is a reversible dehydration reaction. The enzyme requires a divalent metal cation for activation. Primarily it uses Mg^2+ as a cofactor, but some other divalent metal cations are possible. The binding of the cation to the enzyme causes it to undergo a conformational change that allows the substrate to enter the enzyme for conversion. | + | Enolase is an important enzyme for all cells. It is used in glycolysis to catalyze the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP) in the 9th reaction in glycolysis. This reaction is a reversible dehydration reaction. The enzyme requires a divalent metal cation for activation. Primarily it uses Mg^2+ as a cofactor, but some other divalent metal cations are possible. The binding of the cation to the enzyme causes it to undergo a conformational change that allows the substrate to enter the enzyme for conversion. |
| + | ==PDB Sum Info== | ||
2PBD ID: 2AKZ, 1KKO, 4JN7, | 2PBD ID: 2AKZ, 1KKO, 4JN7, | ||
Organism:Agrobacterium radiobacter | Organism:Agrobacterium radiobacter | ||
Revision as of 17:51, 16 October 2013
|
| 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. |
To get started:
More help: Help:Editing |
Introduction
Enolase is an important enzyme for all cells. It is used in glycolysis to catalyze the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP) in the 9th reaction in glycolysis. This reaction is a reversible dehydration reaction. The enzyme requires a divalent metal cation for activation. Primarily it uses Mg^2+ as a cofactor, but some other divalent metal cations are possible. The binding of the cation to the enzyme causes it to undergo a conformational change that allows the substrate to enter the enzyme for conversion.
PDB Sum Info
2PBD ID: 2AKZ, 1KKO, 4JN7, Organism:Agrobacterium radiobacter Molecules bound: Na and L-Malate
Catalytic Residues: E166, H189, E209, V240,K342, H370, K393 Ligands: G37, A38, S39, T40, I42, H157, Q165, E166, E209, S248, E249, Q297, K342, R371, S372 Metal binding sites: S39, Q165, E166, D244, E242, D317, L340, K342, K393 Oligometric State: dimer
Enzymatic reaction: 2-phopsho-D-glycerate (w/ Mg)<--> phosphoenolpyruvate + water
is an a cool enzyme
. This shows the alpha-helices in blue, and the beta-sheets in orange, as well as the non-repetitive structure in white
has lots of cool alpha-helices
is displayed here in red.
Because the beta-sheets are parallel, the H-bonds are not direct or straight, and therefore not as strong.
are shown in gray. These residues prefer little to no contact with water, and so typically hide in the interior of the protein
are shown in purple. These residues prefer contact with water, and so typically appear on the surface of the protein
surrounding Enolase only reacts with the hydrophilic residues of the protein and forces the hydrophobic residues into the interior to minimize contact with them and so water can increase its own entropy.
are displayed in yellow. The majority of the residues binding with the Ligand include Serine, Glutamic acid, and Aspartic acid.
are shown here in lime green. These are the residues of the enzyme's active site that are reported to also interact with the non-hydrolysable substrate.
