Enolase superfamily

The reactions catalyzed by enzymes in the enolase superfamily share the core chemical step of an abstraction of a proton from a carbon adjacent to a carboxylic acid and a requirement of a divalent metal ion. In contrast to many recognized families of enzymes whose members catalyze similar reactions on different substrates, the enolase superfamily includes enzymes catalyzing a wide variety of reactions and performing diverse roles in metabolism.

Members

• enolase
• mandelate racemase (MR)
• muconate lactonizing enzyme (MLE)

The primary sequences of MR and MLE, approximately 25% identical, are related but significantly different; whereas their three-dimensional structures are similar. The enzyme enolase has a more distant, but nevertheless clear, relationship to MLE and MR. The enolase superfamily has served as a model superfamily for understanding enzyme function and is one of the protein families under study by the Enzyme Function Initiative (EFI).

External links

• Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase.
• Enolase Superfamily overview from the EFI