1509-81-5Relevant articles and documents
Rescue of K12G triosephosphate isomerase by ammonium cations: The reaction of an enzyme in pieces
Go, Maybelle K.,Amyes, Tina L.,Richard, John P.
, p. 13525 - 13532 (2010)
The K12G mutation at yeast triosephosphate isomerase (TIM) results in a 5.5 × 105-fold decrease in kcat/Km for isomerization of glyceraldehyde 3-phosphate, and the activity of this mutant can be successfully rescued by NH4+ and primary alkylammonium cations. The transition state for the K12G mutant TIM-catalyzed reaction is stabilized by 1.5 kcal/mol by interaction with NH4 +. The larger 3.9 kcal/mol stabilization by CH3CH 2CH2CH2NH3+ is due to hydrophobic interactions between the mutant enzyme and the butyl side chain of the cation activator. There is no significant transfer of a proton from alkylammonium cations to GAP at the transition state for the K12G mutant TIM-catalyzed reaction, because activation by a series of RNH3 + shows little or no dependence on the pKa of RNH 3+. A comparison of kcat/Km = 6.6 × 106 M-1 s-1 for the wildtype TIM-catalyzed isomerization of GAP and the third-order rate constant of 150 M-2 s-1 for activation by NH4+ of the K12G mutant TIM-catalyzed isomerization shows that stabilization of the bound transition state by the effectively intramolecular interaction of the cationic side chain of Lys-12 at wildtype TIM is 6.3 kcal/mol greater than that for the corresponding intermolecular interaction of NH4+ at K12G mutant TIM.
Carbohydrates from glycerol: An enzymatic four-step, one-pot synthesis
Schoevaart, Rob,Van Rantwijk, Fred,Sheldon, Roger A.
, p. 2465 - 2466 (1999)
A novel one-pot procedure, involving a cascade of four enzymatic steps, for the synthesis of carbohydrates from glycerol and an aldehyde is reported.
An efficient chemoenzymatic route to dihydroxyacetone phosphate from glycidol for the in situ aldolase-mediated synthesis of monosaccharides
Charmantray, Franck,Dellis, Phillipe,Samreth, Soth,Hecquet, Laurence
, p. 3261 - 3263 (2006)
We report a new two-step procedure that uses inexpensive rac-glycidol to obtain valuable dihydroxyacetone phosphate (DHAP), a building block for the synthesis of monosaccharide analogues.
The first nonradioactive fluorescence assay for phosphatidylglycerol: prolipoprotein diacylglyceryl transferase that initiates bacterial lipoprotein biosynthesis
Sundaram, Srividhya,Banerjee, Sanchari,Sankaran, Krishnan
, p. 163 - 170 (2012)
The unique and physiologically vital bacterial enzyme, prolipoprotein diacylglyceryl transferase (Lgt), which catalyzes the committed first step in the posttranslational transfer of diacylglyceryl group from phosphatidylglycerol to the prospective N-terminal cysteine of prolipoproteins, remains to be characterized for want of a simpler but equally sensitive nonradioactive assay. We, for the first time, report a coupled enzymatic fluorescence assay for Lgt using the de novo synthetic peptide substrate MKATKSAVGSTLAGCSSHHHHHH. The assay is based on the conversion of the by-product, glycerol-1-phosphate, to dihydroxyacetone using an alkaline phosphatase-glycerol dehydrogenase combination and estimating the fluorescence of the coupled reduction of resazurin to resorufin. The minimum amount of glycerol-1-phosphate, and hence the modified peptide, detected by this method is approximately 20 pmol, thereby making this assay a promising alternative to the radioactive assays. The assay is rapid, more convenient, less laborious, and suitable for purification and characterization of Lgt.
Darwin's Warm Little Pond: A One-Pot Reaction for Prebiotic Phosphorylation and the Mobilization of Phosphate from Minerals in a Urea-Based Solvent
Burcar, Bradley,Pasek, Matthew,Gull, Maheen,Cafferty, Brian J.,Velasco, Francisco,Hud, Nicholas V.,Menor-Salván, César
, p. 13249 - 13253 (2016)
The poor reactivity of insoluble phosphates, such as apatite-group minerals, has been a long-appreciated obstacle for proposed models of prebiotic organophosphate formation. This obstacle presents a significant challenge to the nascent development of an RNA world and other models for the origins of life on Earth. Herein, we demonstrate that a scenario based on the formation of a urea/ammonium formate/water (UAFW) eutectic solution leads to an increase in phosphorylation when compared to urea alone for phosphate sources of varying solubility. In addition, under evaporative conditions and in the presence of MgSO4, the UAFW eutectic mobilizes the phosphate sequestered in water-insoluble hydroxyapatite, giving rise to a marked increase in phosphorylation. These results suggest that the prebiotic concentrations of urea in a geologically plausible evaporitic environment could solve the problem of organic phosphorylation on a prebiotic Earth.
A toothpaste additive CGP new synthetic process of the (by machine translation)
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Paragraph 0041-0047, (2018/09/28)
The invention relates to a toothpaste additive new synthetic process of the CGP, specifically comprising the following steps: (1) under ice bath, is added to the glycerin in the POCl3 And catalyst, natural recovery to room temperature, stirring the reaction 5 - 6 h after, adds full and sodium bicarbonate solution adjusted to pH 8.0 - 9.0 after, adding calcium chloride, stirring at room temperature the reaction 10 - 12 hours, filter, collecting the filtrate; (2) to the step (1) of the filtrate obtained in adding anhydrous ethanol, stirring 0.5 - 1.0 h after, filtering, deposition and drying to obtain the CGP. (by machine translation)
Novel synthetic method to synthesize intermediate glycerophosphate from calcium glycerophosphate
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Paragraph 0042; 0043; 0044; 0045, (2018/10/19)
The invention relates to a novel synthetic method to synthesize intermediate glycerophosphate from calcium glycerophosphate, comprising the steps: adding glycerol into POCl3 and a catalyst under ice bath, allowing natural restoring to room temperature, stirring to allow reaction for 5-6 h, distilling in vacuum, and collecting glycerophosphate fraction. The catalyst is ionic-liquid-modified silica-supported pyrophosphoric acid catalyst.
Biocide compositions comprising glycerol(ether)phosphates
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, (2011/10/12)
Suggested are biocide compositions, comprising (a) Glycerol(ether)phosphates; (b) Biocides and optionally (c) Oil components or co-solvents and/or (d) Emulsifiers. The compositions show excellent adjuvant and complexing properties.
Resolving the enigma of prebiotic C-O-P bond formation: Prebiotic hydrothermal synthesis of important biological phosphate esters
Maheen, Gull,Tian, Ge,Wang, Yingwu,He, Chao,Shi, Zhan,Yuan, Hongming,Feng, Shouhua
scheme or table, p. 161 - 167 (2011/06/28)
Important biological phosphate esters such as sn-glycerol-3-phosphate, glycerol-2- phosphate, and phosphoethanolamine were synthesized under hydrothermal conditions. Phosphorus was incorporated into the biomolecules, leading to the formation of C-O-P type compounds hydrother- mally. Only perlite-catalyzed reaction at 180° C could result in the formation of sn-glycerol-3-phosphate, whereas glycerol-2-phosphate could be easily synthesized at 100°C with or without minerals and phos- phoethanolamine was obtained within a temperature range of 100 to 120°.
Regioselective phosphorylation of carbohydrates and various alcohols by bacterial acid phosphatases; probing the substrate specificity of the enzyme from Shigella flexneri
Van Herk, Teunie,Hartog, Aloysius F.,Van Der Burg, Alida M.,Wever, Ron
, p. 1155 - 1162 (2007/10/03)
Bacterial non-specific acid phosphatases normally catalyze the dephosphorylation of a variety of substrates. As shown previously the enzymes from Shigella flexneri and Salmonella enterica are also able to catalyze the phosphorylation of inosine to inosine monophosphate and D-glucose to D-glucose 6-phosphate (D-G6P) using cheap pyrophosphate as the phosphate donor. After optimization high yields (95%) are achieved in the latter reaction and we show here that it is possible to use these enzymes in a preparative manner. This prompted us to investigate by using 31P NMR and HPLC also the phosphorylation of a broad range of carbohydrates and alcohols. Many cyclic carbohydrates are phosphorylated in a regioselective manner. Non-cyclic carbohydrates are phosphorylated as well. Phosphorylation of linear alcohols, cyclic and aromatic alcohols is also possible. In all cases the acid phosphatase from Shigella prefers a primary alcohol function above a secondary one. We conclude that these enzymes are an attractive alternative to existing chemical and enzymatic methods in the phosphorylation of a broad range of compounds.
