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Neuron Specific Enolase (Enolase 2)

Introduction

Biological Assembly Image for 1PDY Lobster Enolase ^[3]

Enolase has three subunits (α, β, and γ) and all of these subunits are usually found in vertebrates. Enolase α is ubiquitous, found in all cells, enolase β is muscle-specific, and the γ isozyme is found only in neurons.^[4] The subunits can combine in pairs (αα, αβ, αγ, ββ, and γγ) and form the five different isozymes of enolase. It is more common to find the homodimers (αα, ββ, and γγ) in adult human cells. The αα is called enolase 1, the ββ enolase 3, and the γγ enolase 2. Each homodimer still holds their original function: Enolase 1 is non-neuronal enolase (NNE), which is found in a variety of tissues, including liver, brain, kidney, spleen, adipose, enolase 3 is muscle specific enolase (MSE), and enolase 2 neuron-specific enolase (NSE). ^[1]

NSE (also called Gamma-Enolase) is the most abundant form of the glycolytic enolase found in adult neurons and is thought to serve as a growth factor in neurons. NSE is useful in studying neuronal differentiation and is, therefore, a valuable tool for visualizing the entire neuron and endocrine systems. ^[5] NSE is mainly found in mammals, and it functions as a Phosphopyruvate dehydratase. It is specifically a hydro-lyase, which cleave carbon-oxygen bonds. In humans, NSE is encoded by the ENO2 gene.^[6] The systematic name of this enzyme class is 2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming). Other names in common use include nervous-system specific enolase, phosphoenolpyruvate hydrates, 2-phosphoglycerate dehydrates, 2-phosphoglyceric dehydrates, gamma-enolase, and 2-phospho-D-glycerate hydro-lyase. The only inhibitor known for the enzyme so far is Phosphonoacetohydroxamate ^[7]

Structure

NSE, as mentioned in the introduction, is composed of the two gamma, γ, subunits of enolase. NSE functions in neurons, but it still performs the duties of glycolytic enolase. Each subunit is composed of two domains, a smaller N-terminal Domain and a larger C-terminal domain. For enolase in general, the smaller N-terminal domain consists of three α-helices and four β-sheets. The larger C-terminal domain starts with two β-sheets followed by two α-helices and ends with a barrel composed of alternating β-sheets and α-helices arranged so that the β-beta sheets are surrounded by the α-helices. The enzyme’s compact, globular structure results from significant hydrophobic interactions between these two domains. ^[1]

Biological Assembly Image for 1TE6 Enolase 2 ^[8]

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Mechanism

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Medicine

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References

1. ↑ ^{1.0 1.1 1.2 1.3} http://en.wikipedia.org/wiki/Enolase
2. ↑ http://en.wikipedia.org/wiki/Metalloenzyme#Metalloenzymes
3. ↑ X-RAY STRUCTURE AND CATALYTIC MECHANISM OF LOBSTER ENOLASE: http://www.rcsb.org/pdb/explore/explore.do?structureId=1PDY
4. ↑ Stopped-flow studies of the reaction of d-tartronate semialdehyde-2-phosphate with human neuronal enolase and yeast enolase 1: http://www.sciencedirect.com.prox.lib.ncsu.edu/science/article/pii/S0014579310000657
5. ↑ Neuron Specific Enolase: http://www.scrippslabs.com/cancer-markers-neuron-specific-enolase-nse/
6. ↑ http://en.wikipedia.org/wiki/Enolase_2
7. ↑ http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase
8. ↑ Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom: http://www.rcsb.org/pdb/explore/explore.do?structureId=1te6