enolase

Genetics is found to be the cause of enolase deficiency.

Enolase is bound to the surface of P. falciparum and several other pathogens.

Gamma-enolase is one of the three enolase isoenzymes found in mammals.

Fluoride has a direct inhibitory effect on the enolase enzyme.

These were found in two essential cellular proteins elongation factor l and enolase.

PEP is formed by the action of the enzyme enolase on 2-phosphoglycerate.

Enolase is present in all tissues and organisms capable of glycolysis or fermentation.

Enolase can also catalyze the reverse reaction, depending on environmental concentrations of substrates.

Also known as enolase 3.

Enolase is a highly conserved enzyme with five active-site residues being especially important for activity.

Fluoride is a known competitor of enolase's substrate 2-PG.

The gene for Enolase 1 has been localized to Chromosome 1 in humans.

This enzyme belongs to the enolase superfamily.

Enolase belongs to the class Lyase.

Mg may also serve in a structural maintenance role in these enzymes (e.g. enolase).

In adult humans, the ββ homodimer accounts for more than 90% of total enolase activity in muscle.

Increased levels of enolase have also been identified in patients who have suffered a recent myocardial infarction or cerebrovascular accident.

The enolase enzyme catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate; this is the ninth step in glycolysis.

The bacterial MLEs belong to the enolase superfamily, several structures from which are known.

Neuron-specific enolase and axonal heavy chain neurofilament blood markers may predict conversion to affected status.

An integral part of enolase are two Mg cofactors in the active site, which serve to stabilize negative charges in the substrate.

Immunohistochemistry reveals the presence of neuron-specific enolase (NSE) and chromogranin.

The same study showed that the fastest rate of tumor growth occurred in patients with the highest levels of CSF enolase.

Enolase is a dimeric protein formed from three subunits, α, β, and γ, encoded by different genes.

Neuron-specific enolase (NSE) is less specific.