Disease relevance of phosphoglycerate

• E211Q, a site-specific variant of enolase that catalyzes the exchange of the alpha-proton of 2-phospho-D-glycerate but not the complete dehydration, was assayed in a (1)H/(2)H exchange reaction at different pDs [1].
• Enolase (2-phospho-D-glycerate hydrolase; EC 4.2.1.11) from the hyperthermophilic bacterium Thermotoga maritima was purified to homogeneity [2].
• A cDNA encoding maize enolase (2-phospho-D-glycerate hydrolase) was purified by functional genetic complementation using an enolase deficient mutant of Escherichia coli, DF261 [3].
• The gamma-subunit of 2-phospho-D-glycerate hydrolyase, E.C. 4.2.1.11 (enolase), neuron-specific enolase (NSE), is present at high concentrations in neurons and neuroendocrine cells and has therefore recently been introduced as a marker for neuroendocrine tumors [4].

High impact information on phosphoglycerate

• During the induction of Crassulacean acid and metabolism by environmental stresses in the common ice plant (Mesembryanthemum crystallinum L.), enzyme activities involved in glycolysis and gluconeogenesis, including enolase (2-phospho-D-glycerate hydrolase), increase significantly [5].
• Yeast enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) has been crystallized by vapor diffusion and equilibrium dialysis of solutions of ammonium sulfate [6].
• The isomerization of 3-phospho-D-glycerate and 2-phospho-D-glycerate catalyzed by the cofactor-independent phosphoglycerate mutase from wheat germ (the isolation and crystallization of which is described in the Appendix) has been shown to be intramolecular by two methods [7].
• The amino-acid sequence deduced from the nt sequence is similar to several eukaryotic 2-phospho-D-glycerate hydrolases (EC 4.2.1.11) [8].
• We report the presence and distribution of alpha (ubiquitous) and gamma (neuron-specific) subunits of the dimeric glycolytic enzyme enolase (2-phospho-D-glycerate hydrolase) in cultured neural cells [9].

Biological context of phosphoglycerate

• Enolase (2-phospho-D-glycerate hydrolase, EC 4.2.1.11) has been identified as an anaerobic stress protein in Echinochloa oryzoides based on the homology of its internal amino acid sequence with those of enolases from other organisms, by immunological reactivity, and induction of catalytic activity during anaerobic stress [10].

Anatomical context of phosphoglycerate

• Four forms (alpha alpha, beta beta, gamma gamma and alpha gamma) of enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) were purified from human brain and skeletal muscle [11].

Associations of phosphoglycerate with other chemical compounds

• The equilibrium mixture of yeast enolase with substrate, 2-phospho-D-glycerate (2-PGA), and product, phosphoenolpyruvate (P-enolpyruvate), has been crystallized from solutions of poly(ethylene glycol) (PEG) at pH 8 [12].
• Crystals have been successfully transferred to an artificial mother liquor, pH = 7.8, 20 mM in Mg(2+) and 5 mM in 2-phospho-D-glycerate [13].
• Yeast enolase (2-phospho-D-glycerate hydrolyase, E.C. 4.2.1.11) has been crystallized by vapor diffusion from a solution containing 22% PEG 4000, 100 mM Tris buffer pH = 9.3, 200 mM Li(2)SO(4) [13].
• Titration of Mg2+ with enolase in the presence of 2-phosphoglycerate (PGA) and Zn2+, where Zn2+ binds specifically at site I, gives a 1/T2 for Mg2+ bound at site II of 4000 s-1 (chi = 0.49 MHz) [14].
• Muscle enolase (2-phospho-D-glycerate hydrolase, EC 4.2.1.11) and liver enolse from young and old rats have been purified to homogeneity and several properties of the respective young/old pairs, including Km, behavior on polyacrylamide gels, sensitivity to heat and specific activity have been compared [15].

Gene context of phosphoglycerate

• In higher vertebrates, the glycolytic enzyme enolase (2-phospho-D-glycerate hydrolyase; EC 4.2.1.11) is active as a dimeric protein formed from three subunits--alpha: ubiquitous, beta: muscle specific, and gamma: neuron specific--encoded by different genes [16].
• When a purified preparation of rat alpha gamma enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) was applied to a chromatofocusing column, the enolase was almost completely dissociated and recombined to form alpha alpha and gamma gamma enolases, which were eluted at different fractions from the column [17].
• The cross-reacting antigens were isolated and characterised as glyceraldehyde-3-phosphate dehydrogenase and 2-phospho-D-glycerate hydrolyase [18].
• 1. The chromatography of rat brain enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) reveals three distinet components [19].

References