Disease relevance of eno

• Initially, with a low-copy-number vector, two E. coli glycolytic gene promoters (gap and eno) were tested and found to be less effective than the original celZ promoter [1].
• Molecular characterization of the Zymomonas mobilis enolase (eno) gene [2].
• The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step [3].
• The recognition site is well conserved in RNase E homologues in a subfamily of the gamma-proteobacteria, including enzymes from pathogens such as Yersinia pestis, Vibrio cholera and Salmonella sp. We suggest that enolase is recruited into putative RNA degradosome machinery in these bacilli, where it plays common regulatory functions [4].
• These E. coli recombinants were shown to express the chlamydia proteins, enolase, pmpD and CT579 [5].

High impact information on eno

• RhlB helicase rather than enolase is the beta-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)-exoribonucleolytic complex [6].
• The RNA degradosome of Escherichia coli is a ribonucleolytic multienzyme complex containing RNase E, polynucleotide phosphorylase, RhlB, and enolase [7].
• The fusion protein phosphorylated endogenous substrates and enolase primarily on serine and threonine [8].
• In immune complex kinase assays, the yeast pp60v-src was autophosphorylated on tyrosine and was able to phosphorylate exogenous substrates such as casein and enolase [9].
• When anaerobically grown E. coli cells were exposed to hydrogen peroxide stress, alcohol dehydrogenase E, elongation factor G, the heat shock protein DNA K, oligopeptide-binding protein A, enolase, and the outer membrane protein A were identified as the major protein targets [10].

Chemical compound and disease context of eno

• Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli [11].
• Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli [12].
• 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 [13].
• Glyceraldehyde 3-p dehydrogenase, glycerate 3-P kinase and enolase mutants of Escherichia coli: genetic studies [14].

Biological context of eno

• Nucleotide sequence analysis of the eno region revealed an open reading frame of 1,293 bp that encodes a protein of 428 amino acids with a predicted molecular weight of 45,813 [2].
• The eno gene is present in a single copy of the Z. mobilis genome [2].
• Unlike all of the previously studied glycolytic genes from Z. mobilis that possess canonical ribosome binding sites, the eno gene is preceded by a modest Shine-Dalgarno sequence [2].
• Results from this and previous studies show that all of the structural genes of the L-fucose trunk pathway map between eno and argA at minute 60.2 of the chromosome [15].
• Nucleotide sequence analysis revealed the presence of a potential operon with the gene order pyrG, kdsA, eno [16].

Associations of eno with chemical compounds

• Phosphoenolpyruvate is one of the substrates for Kdo-8-P biosynthesis by KdsA and cytidine triphosphate is the nucleotide used to activate Kdo prior to its transfer to lipid A. pyrG and eno are important for many metabolic pathways and it is interesting to find them linked to kdsA [16].
• The amounts of eno mRNA when the bacterium was grown on glycerol or glucose were compared to that when D. vulgaris was grown on lactate [17].
• Fluoride inhibition of enolase: crystal structure and thermodynamics [18].
• In vitro labeling of cell extracts from glucose and acetate grown cells resulted in differential labeling of enolase [19].
• In this article, we report the results of an analysis of the glycolytic enzyme enolase (2-phospho-d-glycerate hydrolase) of Trypanosoma brucei [20].

Physical interactions of eno

• A single molecule of the RNase E peptide binds asymmetrically in a conserved cleft at the interface of the enolase dimer [4].

Other interactions of eno

• The triose phosphate isomerase and enolase from B. subtilis are extremely similar to those from all other species, both eukaryotic and prokaryotic [21].
• When 32P-labeled enolase from glucose grown cells was subjected to treatment with potato acid phosphatase, dephosphorylation of the enzyme could be observed [19].
• RNase G-dependent degradation of the eno mRNA encoding a glycolysis enzyme enolase in Escherichia coli [22].

Analytical, diagnostic and therapeutic context of eno

• Using affinity chromatography, we found that PNPase-alpha and RhlB form a ribonucleolytically active complex corresponding to the mass calculated previously for alpha(3)beta(2) (i.e., 377-380 kDa), whereas no association between PNPase-alpha and enolase was detected [6].
• To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase [23].
• Highly sensitive immunoassays for three forms of rat brain enolase [24].
• Highly sensitive enzyme immunoassay systems for three forms (alpha alpha, alpha gamma, and gamma gamma) of rat brain enolase were prepared by use of specific antisera to two distinct subunits (alpha and gamma) of the isozymes and beta-D-galactosidase from Escherichia coli as label [24].
• Northern-blot analysis showed a five-fold anaerobic induction in enolase mRNA, while heat shock or cold shock increased enolase mRNA levels only slightly [13].

References