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Showing 1-27 of 27 results for "19710" within Papers
M J Kornblatt et al.
Yeast (Chichester, England), 30(2), 55-69 (2013-01-30)
In addition to two genes (ENO1 and ENO2) known to code for enolase (EC4.2.1.11), the Saccharomyces cerevisiae genome contains three enolase-related regions (ERR1, ERR2 and ERR3) which could potentially encode proteins with enolase function. Here, we show that products of
Grégory Boël et al.
Journal of molecular biology, 337(2), 485-496 (2004-03-09)
We observed that in vivo and in vitro a small fraction of the glycolytic enzyme enolase became covalently modified by its substrate 2-phosphoglycerate (2-PG). In modified Escherichia coli enolase, 2-PG was bound to Lys341, which is located in the active
C K Brown et al.
Journal of protein chemistry, 17(8), 855-866 (1999-02-13)
Purified enolase from Bacillus subtilis has a native mass of approximately 370 kDa. Since B. subtilis enolase was found to have a subunit mass of 46.58 kDa, the quaternary structure of B. subtilis is octameric. The pl for B. subtilis
Bo Liu et al.
Biotechnology letters, 31(12), 1937-1941 (2009-08-20)
A glycerate kinase gene (ST2037) from the hyperthermophilic crenarchaeon Sulfolobus tokodaii was cloned and expressed in Escherichia coli. The purified homodimeric protein (45 kDa) specifically catalyzed the formation of 2-phosphoglycerate with D-glycerate as substrate. The thermostable enzyme displayed maximum activity
R Götz et al.
Yeast (Chichester, England), 15(15), 1619-1629 (1999-11-26)
Numerous individual enzymes participate in a given synthetic or degradative pathway in which the product of one reaction becomes the substrate for the subsequent enzyme. This raises the question of whether the product of one 'soluble' enzyme diffuses freely through
Sampathkumar Parthasarathy et al.
The Journal of biological chemistry, 278(52), 52461-52470 (2003-10-18)
Triose-phosphate isomerase, a key enzyme of the glycolytic pathway, catalyzes the isomerization of dihydroxy acetone phosphate and glyceraldehyde 3-phosphate. In this communication we report the crystal structure of Plasmodium falciparum triose-phosphate isomerase complexed to the inhibitor 2-phosphoglycerate at 1.1-A resolution.
Peter B A Blomberg et al.
Mathematical biosciences, 220(2), 81-88 (2009-05-12)
Gibbs free energy is the thermodynamic potential representing the fundamental equation at constant temperature, pressure, and molar amounts. Transformed Gibbs energies are important for biochemical systems because the local concentrations within cell compartments cannot yet be determined accurately. The method
Jie Qin et al.
Journal of inorganic biochemistry, 111, 187-194 (2012-03-23)
In the presence of magnesium, enolase catalyzes the dehydration of 2-phospho-d-glycerate (PGA) to phosphoenolpyruvate (PEP) in glycolysis and the reverse reaction in gluconeogensis at comparable rates. The structure of human neuron specific enolase (hNSE) crystals soaked in PGA showed that
D Hakobyan et al.
Biochemistry. Biokhimiia, 71(4), 370-375 (2006-04-18)
Two glycolytic enzymes, phosphoglycerate mutase (PGM) and enolase from Saccharomyces cerevisiae, have been chosen to detect complex formation and possible channeling, using molecular dynamics simulation. The enzymes were separated by 10 angstroms distance and placed in a water-filled box of
Xingjue Xu et al.
Drug design and discovery, 18(2-3), 91-99 (2003-12-17)
3-Deoxy-D-manno-octulosonate 8-phosphate (KDO8P) is the phosphorylated precursor of KDO, an essential sugar of the lipopolysaccharide of Gram negative bacteria. KDO8P is produced by a specific synthase (KDO8PS) by condensing arabinose 5-phosphate (A5P) and phosphoenolpyruvate (PEP), with release of inorganic phosphate.
Liangchun Yang et al.
Nature communications, 5, 4436-4436 (2014-07-16)
Increasing evidence suggests the important role of metabolic reprogramming in the regulation of the innate inflammatory response, but the underlying mechanism remains unclear. Here we provide evidence to support a novel role for the pyruvate kinase M2 (PKM2)-mediated Warburg effect
Emanuela Polidori et al.
Fungal genetics and biology : FG & B, 41(2), 157-167 (2004-01-21)
Enolase from Tuber borchii mycelium was purified to electrophoretical homogeneity using an anion-exchange and a gel permeation chromatography. Furthermore, the corresponding gene (eno-1) was cloned and characterized. The purified enzyme showed a higher affinity for 2-PGA (0.26 mM) with respect
Xiangan Han et al.
Molecular biology reports, 39(3), 2705-2711 (2011-06-16)
Brucella abortus is the etiological agent of brucellosis, a disease causing human public health problems as well as major economic losses in domestic animal industries. In this study, the enolase gene of B. abortus A19 was cloned, sequenced and expressed
Taro Hitosugi et al.
Cancer cell, 22(5), 585-600 (2012-11-17)
It is unclear how cancer cells coordinate glycolysis and biosynthesis to support rapidly growing tumors. We found that the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1), commonly upregulated in human cancers due to loss of TP53, contributes to biosynthesis regulation in
Nicolas Frey et al.
FEMS microbiology letters, 224(1), 67-72 (2003-07-12)
Phosphorylation of HPr, the small phosphocarrier protein of the phosphoenolpyruvate:sugar phosphotransferase system, on Ser46 by the HPr(Ser) kinase (HPrK/P) is a vital step in catabolite repression in Gram-positive bacteria. Streptococcus salivarius HPrK/P is reported to be a multimeric protein not
Zhiru Li et al.
Veterinary parasitology, 176(4), 350-356 (2011-02-18)
Drug treatments for heartworm disease have not changed significantly in the last decade. Due to concerns about possible drug resistance and their lower efficacy against adult worms, there is a need for the development of new antifilarial drug therapies. The
A Keller et al.
Biochimica et biophysica acta, 1770(6), 919-926 (2007-03-21)
Enolase is a glycolytic enzyme, expressed as cell-type specific isoforms in higher vertebrates. Herein we demonstrated for the first time that enolase isoforms interact with microtubules during muscle satellite cell differentiation. While in undifferentiated myoblasts the ubiquitous alphaalpha enolase isoform
D A Vinarov et al.
Biochemistry, 37(43), 15238-15246 (1998-10-28)
The pH dependence of the chemical shifts of the 31P resonances of enzyme-bound substrates 2-phosphoglycerate (PGA) and phosphoenolpyruvate (PEP) were measured to obtain further insight into the catalytic mechanism of yeast enolase. The 31P resonances of PGA and PEP bound
M J Jedrzejas et al.
The Journal of biological chemistry, 275(30), 23146-23153 (2000-04-15)
The structure of the complex between the 2, 3-diphosphoglycerate-independent phosphoglycerate mutase (iPGM) from Bacillus stearothermophilus and its 3-phosphoglycerate substrate has recently been solved, and analysis of this structure allowed formulation of a mechanism for iPGM catalysis. In order to obtain
Keri Lyn Ross et al.
Analytical chemistry, 81(10), 4021-4026 (2009-04-10)
A method has been developed for rapid quantification of nine glycolytic intermediates using ultraperformance liquid chromatography/electrospray-tandem mass spectrometry (UPLC/ESI-MS/MS) to monitor the metabolism of glucose during microbial fermentation. Because comprehensive chromatographic separation is not required, analysis time is significantly less
Bo Liu et al.
Extremophiles : life under extreme conditions, 11(5), 733-739 (2007-06-15)
A glycerate kinase (GK) gene (PH0495) from the hyperthermophilic archaeon Pyrococcus horikoshii, was cloned and expressed in Escherichia coli. The recombinant protein was purified to homogeneity by affinity chromatography and ion exchange chromatography. The enzyme was likely a homodimer based
Somnath Mukherjee et al.
Biochimie, 94(12), 2532-2544 (2012-07-21)
Staphylococcus aureus is one of the most dreaded pathogens worldwide and emergence of notorious antibiotic resistant strains have further exacerbated the present scenario. The glycolytic enzyme, triosephosphate isomerase (TIM) is one of the cell envelope proteins of the coccus and
Takashi Nishimura et al.
Molecular microbiology, 68(1), 98-109 (2008-03-04)
The cmp operon of the cyanobacterium Synechococcus elongatus strain PCC 7942, encoding the subunits of the ABC-type bicarbonate transporter, is activated under CO2-limited growth conditions in a manner dependent on CmpR, a LysR family transcription factor of CbbR subfamily. The
R R Poyner et al.
Biochemistry, 40(27), 8009-8017 (2001-07-04)
Spectroscopic and kinetic methods have been used to explore the roles of divalent metal ions in the enolase-catalyzed dehydration of 2-phosphoglycerate (2-PGA). Enolase requires 2 equiv of metal ion per active site for maximal activity. Previous crystallographic studies [Larsen, T.
Matthias Reher et al.
FEMS microbiology letters, 259(1), 113-119 (2006-05-11)
Picrophilus torridus has been shown to degrade glucose via a nonphosphorylative Entner-Doudoroff (ED) pathway. Here we report the characterization of a key enzyme of this pathway, glycerate kinase (2-phosphoglycerate forming). The enzyme was purified 5,100-fold to homogeneity. The 95 kDa
Zhixin Zhao et al.
Journal of experimental botany, 62(14), 5179-5189 (2011-08-05)
Stomatal movements require massive changes in guard cell osmotic content, and both stomatal opening and stomatal closure have been shown to be energy-requiring processes. A possible role for glycolysis in contributing to the energetic, reducing requirements, or signalling processes regulating
Man Song et al.
Antonie van Leeuwenhoek, 108(2), 377-382 (2015-05-24)
A novel cyhalothrin-degrading strain, designated as LM-6(T), was isolated from a cyhalothrin contaminated wastewater sample. The bacterium was found to be Gram stain-negative, non-spore-forming, vibrio-shaped, and motile with a single polar flagellum. Strain LM-6(T) was observed to grow optimally at
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