56742-44-0Relevant articles and documents
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.
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 (2014/05/06)
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.
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.
