scholarly journals The deoxyfluoro-d-glucopyranose 6-phosphates and their effect on yeast glucose phosphate isomerase

1973 ◽  
Vol 131 (1) ◽  
pp. 77-82 ◽  
Author(s):  
Eric M. Bessell ◽  
Peter Thomas
Keyword(s):  
Hydroxyl Groups ◽  
Glucose Phosphate Isomerase ◽  
Hexokinase 2 ◽  
Glucose Phosphate ◽  
Competitive Inhibitors ◽  
Derivatives Of

1. The deoxyfluoro-d-glucopyranose 6-phosphates were prepared from the corresponding deoxyfluoro-d-glucoses and ATP by using hexokinase. 2. 3-Deoxy-3-fluoro- and 4-deoxy-4-fluoro-d-glucose 6-phosphate were substrates for glucose phosphate isomerase, and in addition the products of this reaction, 3-deoxy-3-fluoro- and 4-deoxy-4-fluoro-d-fructose 6-phosphate respectively, were good substrates for phosphofructokinase. 3. Some C-2-substituted derivatives of d-glucose 6-phosphate were found to be competitive inhibitors of glucose phosphate isomerase. 4. The possible role of the hydroxyl groups in the binding of d-glucose 6-phopshate to glucose phosphate isomerase is discussed.

The role of secondary alcoholic groups of D-galacturonan in its degradation with exo-D-galacturonanase

1980 ◽  
Vol 45 (2) ◽  
pp. 427-434 ◽  
Author(s):  
Kveta Heinrichová ◽  
Rudolf Kohn
Keyword(s):  
Acetyl Derivative ◽  
Competitive Inhibitor ◽  
Hydroxyl Groups ◽  
Pectic Acid ◽  
Substrate Complex ◽  
Enzyme Substrate ◽  
The Individual ◽  
Degradation Degree ◽  
Derivatives Of

The effect of exo-D-galacturonanase from carrot on O-acetyl derivatives of pectic acid of variousacetylation degree was studied. Substitution of hydroxyl groups at C(2) and C(3) of D-galactopyranuronic acid units influences the initial rate of degradation, degree of degradation and its maximum rate, the differences being found also in the time of limit degradations of the individual O-acetyl derivatives. Value of the apparent Michaelis constant increases with increase of substitution and value of Vmax changes. O-Acetyl derivatives act as a competitive inhibitor of degradation of D-galacturonan. The extent of the inhibition effect depends on the degree of substitution. The only product of enzymic reaction is D-galactopyranuronic acid, what indicates that no degradation of the terminal substituted unit of O-acetyl derivative of pectic acid takes place. Substitution of hydroxyl groups influences the affinity of the enzyme towards the modified substrate. The results let us presume that hydroxyl groups at C(2) and C(3) of galacturonic unit of pectic acid are essential for formation of the enzyme-substrate complex.

scholarly journals F/OH ratio in a rare fluorine-poor blue topaz from Padre Paraíso (Minas Gerais, Brazil) to unravel topaz’s ambient of formation

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
N. Precisvalle ◽  
A. Martucci ◽  
L. Gigli ◽  
J. R. Plaisier ◽  
T. C. Hansen ◽  
...  
Keyword(s):  
Supercritical Fluids ◽  
Fluorine Content ◽  
Minas Gerais ◽  
Hydroxyl Groups ◽  
Exchange Reactions ◽  
Silicate System ◽  
Mullite Phase ◽  
Anomalous Water

AbstractTopaz [Al2SiO4(F,OH)2] is one of the main fluorine-bearing silicates occurring in environments where variably acidic (F)/aqueous (OH) fluids saturate the silicate system. In this work we fully characterized blue topaz from Padre Paraíso (Minas Gerais, Brazil) by means of in situ synchrotron X-Ray and neutron powder diffraction measurements (temperature range 298–1273 K) combined with EDS microanalyses. Understanding the role of OH/F substitution in topaz is important in order to determine the hydrophilicity and the exchange reactions of fluorine by hydroxyl groups, and ultimately to characterize the environmental redox conditions (H2O/F) required for mineral formation. The fluorine content estimated from neutron diffraction data is ~ 1.03 a.f.u (10.34 wt%), in agreement with the chemical data (on average 10.0 wt%). The XOH [OH/(OH + F)] (0.484) is close to the maximum XOH value (0.5), and represents the OH- richest topaz composition so far analysed in the Minas Gerais district. Topaz crystallinity and fluorine content sharply decrease at 1170 K, while mullite phase starts growing. On the basis of this behaviour, we suggest that this temperature may represent the potential initial topaz’s crystallization temperature from supercritical fluids in a pegmatite system. The log(fH2O/fHF)fluid (1.27 (0.06)) is coherent with the fluorine activity calculated for hydrothermal fluids (pegmatitic stage) in equilibrium with the forming mineral (log(fH2O/fHF)fluid = 1.2–6.5) and clearly different from pure magmatic (granitic) residual melts [log(fH2O/fHF)fluid < 1]. The modelled H2O saturated fluids with the F content not exceeding 1 wt% may represent an anomalous water-dominant / fluorine-poor pegmatite lens of the Padre Paraíso Pegmatite Field.

Anomalous narrowing of the shape of the structural process in derivatives of trehalose at high pressure. The role of the internal structure

2021 ◽  
pp. 116321
Author(s):  
Dawid Heczko ◽  
Joanna Grelska ◽  
Karolina Jurkiewicz ◽  
Patrycja Spychalska ◽  
Anna Kasprzycka ◽  
...  
Keyword(s):  
High Pressure ◽  
Internal Structure ◽  
Structural Process ◽  
Derivatives Of

Characterization of the 5′ end of the gene for human glucose phosphate isomerase (GPI)

Genomics ◽  
1990 ◽  
Vol 7 (4) ◽  
pp. 638-643 ◽  
Author(s):  
James I.H. Walker ◽  
Pelin Faik ◽  
Michael J. Morgan
Keyword(s):  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate

scholarly journals Enzymatic synthesis and phosphorolysis of 4(2)-thioxo- and 6(5)-azapyrimidine nucleosides by E. coli nucleoside phosphorylases

2016 ◽  
Vol 12 ◽  
pp. 2588-2601 ◽  
Author(s):  
Vladimir A Stepchenko ◽  
Anatoly I Miroshnikov ◽  
Frank Seela ◽  
Igor A Mikhailopulo
Keyword(s):  
Purine Nucleoside Phosphorylase ◽  
Reaction Conditions ◽  
E Coli ◽  
No Formation ◽  
Structural Peculiarities ◽  
Substrate Properties ◽  
Nucleoside Phosphorylases ◽  
Derivatives Of

The trans-2-deoxyribosylation of 4-thiouracil (4SUra) and 2-thiouracil (2SUra), as well as 6-azauracil, 6-azathymine and 6-aza-2-thiothymine was studied using dG and E. coli purine nucleoside phosphorylase (PNP) for the in situ generation of 2-deoxy-α-D-ribofuranose-1-phosphate (dRib-1P) followed by its coupling with the bases catalyzed by either E. coli thymidine (TP) or uridine (UP) phosphorylases. 4SUra revealed satisfactory substrate activity for UP and, unexpectedly, complete inertness for TP; no formation of 2’-deoxy-2-thiouridine (2SUd) was observed under analogous reaction conditions in the presence of UP and TP. On the contrary, 2SU, 2SUd, 4STd and 2STd are good substrates for both UP and TP; moreover, 2SU, 4STd and 2’-deoxy-5-azacytidine (Decitabine) are substrates for PNP and the phosphorolysis of the latter is reversible. Condensation of 2SUra and 5-azacytosine with dRib-1P (Ba salt) catalyzed by the accordant UP and PNP in Tris∙HCl buffer gave 2SUd and 2’-deoxy-5-azacytidine in 27% and 15% yields, respectively. 6-Azauracil and 6-azathymine showed good substrate properties for both TP and UP, whereas only TP recognizes 2-thio-6-azathymine as a substrate. 5-Phenyl and 5-tert-butyl derivatives of 6-azauracil and its 2-thioxo derivative were tested as substrates for UP and TP, and only 5-phenyl- and 5-tert-butyl-6-azauracils displayed very low substrate activity. The role of structural peculiarities and electronic properties in the substrate recognition by E. coli nucleoside phosphorylases is discussed.

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