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From Proteopedia

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

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.