enolase


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Related to enolase: glycolysis

enolase

 [e´no-lās]
an enzyme in glycolytic systems that changes phosphoglyceric acid into phosphopyruvic acid.

e·no·lase

(ē'nol-ās),
An enzyme catalyzing the reversible dehydration of 2-phospho-d-glycerate to phosphoenolpyruvate and water; a step in both glycolysis and gluconeogenesis; several isozymes exist; requires magnesium ion and is inhibited by F-.

enolase

/eno·lase/ (e´no-lās) an enzyme that catalyzes the dehydration of 2-phosphoglycerate to form phospho, a step in the pathway of glucose metabolism.
neuron-specific enolase  an isozyme of enolase found in normal neurons and all the cells of the neuroendocrine system; it is a marker for neuroendocrine differentiation in tumors.

enolase

(ē′nə-lās′, -lāz′)
n.
An enzyme that catalyzes one of the steps of glycolysis.

e·no·lase

(ē'nō-lās)
An enzyme catalyzing the reversible dehydration of 2-phospho-d-glycerate to phosphoenolpyruvate and water; a step in both glycolysis and gluconeogenesis; several isozymes exist; requires magnesium ion and is inhibited by F-.

e·no·lase

(ē'nō-lās)
An enzyme catalyzing the reversible dehydration of 2-phospho-d-glycerate to phosphoenolpyruvate and water.

enolase (e´nolās),

n an enzyme characterized by its crystalline structure and role in carbohydrate utilization.

enolase

an enzyme in glycolytic systems that changes phosphoglyceric acid into phosphopyruvic acid.
References in periodicals archive ?
The prognostic value of serum neuron-specific enolase in traumatic brain injury: systematic review and meta-analysis.
For example, in Supplemental Material, Table S3, the enolases were grouped under "Cell growth and function" because of their roles in carbohydrate metabolism and glycolysis, but they also have roles in stress response in neurons (Diaz-Ramos et al.
Neuron specific enolase in neuroendocrine tumors of the thymus, bronchia and skin.
15,16) The positive reaction for neuron-specific enolase and SI00 both confirmed the neuronal origin of the tumor cells.
It measures both neuron-specific enolase (NSE) and Pro-gastrin-releasing peptide (ProGRP), which enhances diagnostic accuracy.
To exclude the different cells origin of this tumor, other immunohistochemical staining were done: pancytokeratin (-), chromogranin A (-), SMA (-), CD117 (-) CD45 (-) Neuron-specific enolase (-) (Fig 1a.
Immunohistochemical staining of the tumor was positive for neuron-specific enolase (NSE) and pancytokeratin AE1/AE3.
Paragangliomas will show positivity for neuron-specific enolase, chromogranin A and synaptophysin as well as S100 protein positivity for sustentacular cells and are negative for thyroglobulin and calcitonin.
Nearly all of the proteins altered in significant amounts were identified as enzymes associated with important metabolic pathways, such as alcohol dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Xaa-His dipeptidase, ornithine carbamoyltransferase, putative O-acetylserine lyase, enolase (2-phosphoglycerate dehydratase), fructose-bisphosphate aldolase, and cysteine synthase.
Several spots were identified (Table I): probable ER-60 luminal cystein protease precursor, superoxide dismutase (Cu-Zn), thioredoxin peroxidase, actin-2, enolase, fructose biphosphate aldolase, Sm28GST, GST-Omega, 30 kD glycoprotein, among others.