17510-99-5Relevant academic research and scientific papers
Substrate specificity and stereoselectivity of two Sulfolobus 2-keto-3-deoxygluconate aldolases towards azido-substituted aldehydes
Schurink, Marloes,Wolterink-Van Loo, Suzanne,Van Der Oost, John,Sonke, Theo,Franssen, Maurice C. R.
, p. 1073 - 1081 (2014)
The 2-keto-3-deoxygluconate aldolases (KDGAs) isolated from Sulfolobus species convert pyruvate and glyceraldehyde reversibly into 2-keto-3-deoxygluconate and -galactonate. As a result of their high thermostability and activity on nonphosphorylated substrates, KDGA enzymes have potential as biocatalysts for the production of building blocks for fine chemical and pharmaceutical applications. Up to now, wild-type enzymes have only shown moderate stereocontrol for their natural reaction. However, if a set of azido-functionalized aldehydes were applied as alternative acceptors in the reaction with pyruvate, the stereoselectivity was strongly increased to give enantiomeric or diastereomeric excess values up to 97 %. The Sulfolobus acidocaldarius KDGA displayed a higher stereoselectivity than Sulfolobus solfataricus KDGA for all tested reactions. The azido-containing products are useful chiral intermediates in the synthesis of nitrogen heterocycles. Taming the wild-type: Two 2-keto-3-deoxygluconate aldolases from Sulfolobus species readily couple azido-substituted aldehydes to pyruvate in a stereoselective manner. The resulting compounds yield chiral nitrogen heterocycles upon reduction.
Synthesis of Furans from Sugars Via Keto Intermediates
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Paragraph 0053, (2018/03/25)
The present invention provides a method of preparing a furan derivative comprising the steps of (a) converting a monosaccharide to provide a keto-intermediate product; and (b) dehydrating the keto-intermediate product to provide a furan derivative; wherein the keto-intermediate product is pre-disposed to forming keto-furanose tautomers in solution. The method may further comprising a step of oxidizing the furan derivative to provide a furandicarboxylic acid or a furandicarboxylic acid derivative.
SYNTHESIS OF FDCA AND FDCA PRECURSORS FROM GLUCONIC ACID DERIVATIVES
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Paragraph 0085, (2017/04/04)
The present invention provides methods of method of synthesizing 2,5-furan dicarboxylic acid (FDCA) and FDCA precursor molecules. The methods involve performing a chemical dehydration reaction on a gluconic acid derivative in the presence of a dehydration catalyst. In some embodiments the gluconic acid derivative can be 2-dehydro-3-deoxy gluconic acid (DHG) or an ester thereof, 2-ketogluconic acid (2KGA) or an ester thereof, and 5-ketogluconic acid (5KGA) or an ester thereof. The 2,5-furan dicarboxylic acid precursor molecule is thereby synthesized, which can be converted into FDCA. The chemical dehydration can be performed by a variety of acid basic catalysts.
Expanding the reaction space of aldolases using hydroxypyruvate as a nucleophilic substrate
De Berardinis, Véronique,Guérard-Hélaine, Christine,Darii, Ekaterina,Bastard, Karine,Hélaine, Virgil,Mariage, Aline,Petit, Jean-Louis,Poupard, Nicolas,Sánchez-Moreno, Israel,Stam, Mark,Gefflaut, Thierry,Salanoubat, Marcel,Lemaire, Marielle
, p. 519 - 526 (2017/08/14)
Aldolases are key biocatalysts for stereoselective C-C bond formation allowing access to polyoxygenated chiral units through direct, efficient, and sustainable synthetic processes. The aldol reaction involving unprotected hydroxypyruvate and an aldehyde offers access to valuable polyhydroxy-α-keto acids. However, this undescribed aldolisation is highly challenging, especially regarding stereoselectivity. This reaction was explored using, as biocatalysts, a collection of aldolases selected from biodiversity. Several enzymes that belong to the same pyruvate aldolase Pfam family (PF03328) were found to produce the desired hexulosonic acids from hydroxypyruvate and d-glyceraldehyde with complementary stereoselectivities. One of them was selected for the proof of concept as a biocatalytic tool to prepare five (3S,4S) aldol adducts through an eco-friendly process.
Validation of the metabolic pathway of the alginate-derived monomer in Saccharophagus degradans 2-40T by gas chromatography–mass spectrometry
Kim, Do Hyoung,Wang, Damao,Yun, Eun Ju,Kim, Sooah,Kim, Soo Rin,Kim, Kyoung Heon
, p. 1374 - 1379 (2016/10/03)
Marine macroalgae are potential resources for the sustainable production of biofuels and bio-based chemicals. Alginate, a major component of brown macroalgae, consists of two uronate monomers, which are further non-enzymatically converted to 4-deoxy-L-erythro-5-hexoseulose uronate (DEH). In several marine bacteria, DEH is known to be metabolized via three enzymatic steps, consisting of DEH reductase, 2-keto-3-deoxy-D-gluconate (KDG) kinase, and 2-keto-3-deoxy-phosphogluconate (KDPG) aldolase, which yields two glycolytic intermediates: D-glyceraldehyde-3-phosphate and pyruvate. However, such functions of these enzymes for the DEH pathway have rarely been experimentally validated. In the present study, the DEH metabolic pathway was investigated in Saccharophagus degradans 2-40T, a marine bacterium that utilizes alginate. Through in vitro tests assisted by gas chromatography/mass spectrometry and gas chromatography/time-of-flight mass spectrometry, the purified enzymes were functionally confirmed and annotated as dehR, kdgK, and kdpgA, respectively. In conclusion, we report the in vitro validation of the metabolic pathway of DEH monomerized from alginate.
Reactivity of thermally treated α-dicarbonyl compounds
Pfeifer, Yvonne V.,Haase, Paul T.,Kroh, Lothar W.
, p. 3090 - 3096 (2013/08/25)
The degradation reaction of thermally treated 3-deoxy-d-erythro-hexos-2- ulose and methylglyoxal, both key intermediates in Maillard chemistry, was investigated. Different analytical strategies were accomplished to cover the broad range of formed products and their different chemical behavior. These involved HPLC-DAD and accordingly LC/MS analysis of the quinoxaline derivates, GC/MS analysis of the acetylated quinoxalines, and GC-FID analysis of the decyl ester of acetic acid. As a main degradation product of 3-deoxy-d-erythro-hexos- 2-ulose, 5-(hydroxymethyl)furfural could be identified. At alkaline pH values, 3-deoxy-d-erythro-hexos-2-ulose generated various acids but no colored products. In contrast, thermal treatment of methylglyoxal yielded high molecular weight, brownish products. A dimer of methylglyoxal, first precursor for aldol-based polymerization of methylglyoxal, could be clearly identified by GC/MS.
Engineering stereocontrol into an aldolase-catalysed reaction
Lamble, Henry J.,Danson, Michael J.,Hough, David W.,Bull, Steven D.
, p. 124 - 126 (2007/10/03)
A novel thermostable aldolase has been developed for synthetic application, and substrate engineering has been used to induce stereocontrol into aldol reactions of this naturally-promiscuous enzyme.
Pyruvate Aldolases as Reagents for Stereospecific Aldol Condensation
Allen, Sarah T.,Heintzelman, Geoffrey R.,Toone, Eric J.
, p. 426 - 427 (2007/10/02)
KDPG aldolase, a representative member of the largest but as of yet unexplored group of aldolases which utilize pyruvate as the nucleophilic component in aldol condensation, accepts a number of unnatural aldehydes as electrophiles in stereospecific aldol condensation, providing access to highly and differentially functionalized α-keto acid products.
