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From Proteopedia

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

Ligand contacts: 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.

is displayed here in green. The ligand for this enzyme is L-malate. The other part of the ligand is Mg cations that will be shown in the next scene.

ions are shown here in blue along with L-malate in green. These two components make up the ligand.

are highlighted here. The residues binding with the Ligand include Ile, Gln, Thr, Glu, and Ser. These residues make sense because they all have the potential to bind with the ligand through hydrogen bonding, either from the backbone or R group

are shown here in light blue. These are the residues of the enzyme's active site that are reported to also interact with the non-hydrolysable substrate. The ligand pieces are displayed as well, with L-malate being lime green and the Mg^2+ ions as dark blue