Biology:Enolase superfamily
The enolase superfamily is a superfamily of enzymes, members of which catalyse a range of reactions. The enolase superfamily includes enzymes that catalyse a wide variety of reactions and performing diverse roles in metabolism. However, the reactions catalysed share the common chemical step of abstraction of a proton from a carbon adjacent to a carboxylic acid and a requirement of a divalent metal ion.[1] This diversity of functions is in contrast to many families of enzymes whose members catalyse similar chemical reactions on different substrates.
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).
References
- ↑ Babbitt, Patricia; Hasson, Miriam; Wedekind, Joseph; Palmer, David; Barrett, William; Reed, George; Rayment, Ivan; Ringe, Dagmar et al. (1996). "The Enolase Superfamily: A General Strategy for Enzyme-Catalyzed Abstraction of the Alpha-Protons of Carboxylic Acids". Biochemistry 51 (35): 16489–16501. doi:10.1021/bi9616413. PMID 8987982.
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
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