24286-28-0Relevant articles and documents
Triacetonide of Glucoheptonic Acid in the Scalable Syntheses of d -Gulose, 6-Deoxy- d -gulose, l -Glucose, 6-Deoxy- l -glucose, and Related Sugars
Liu, Zilei,Yoshihara, Akihide,Jenkinson, Sarah F.,Wormald, Mark R.,Estévez, Ramón J.,Fleet, George W.J.,Izumori, Ken
supporting information, p. 4112 - 4115 (2016/08/30)
Ease of separation of petrol-soluble acetonides derived from the triacetonide of methyl glucoheptonate allows scalable syntheses of rare sugars containing the l-gluco or d-gulo structural motif with any oxidation level at the C6 or C1 position of the hexose, usually without chromatography: meso-d-glycero-d-guloheptitol available in two steps is an ideal entry point for the study of the biotechnological production of heptoses.
Discovery of an l-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily
Hobbs, Merlin Eric,Vetting, Matthew,Williams, Howard J.,Narindoshvili, Tamari,Kebodeaux, Devon M.,Hillerich, Brandan,Seidel, Ronald D.,Almo, Steven C.,Raushel, Frank M.
, p. 239 - 253 (2013/03/13)
A member of the amidohydrolase superfamily, BmulJ-04915 from Burkholderia multivorans, of unknown function was determined to hydrolyze a series of sugar lactones: l-fucono-1,4-lactone, d-arabino-1,4-lactone, l-xylono-1,4-lactone, d-lyxono-1,4-lactone, and l-galactono-1,4-lactone. The highest activity was shown for l-fucono-1,4-lactone with a kcat value of 140 s -1 and a kcat/Km value of 1.0 × 10 5 M-1 s-1 at pH 8.3. The enzymatic product of an adjacent l-fucose dehydrogenase, BmulJ-04919, was shown to be l-fucono-1,5-lactone via nuclear magnetic resonance spectroscopy. l-Fucono-1,5-lactone is unstable and rapidly converts nonenzymatically to l-fucono-1,4-lactone. Because of the chemical instability of l-fucono-1,5-lactone, 4-deoxy-l-fucono-1,5-lactone was enzymatically synthesized from 4-deoxy-l-fucose using l-fucose dehydrogenase. BmulJ-04915 hydrolyzed 4-deoxy-l-fucono-1,5-lactone with a kcat value of 990 s-1 and a kcat/Km value of 8.0 × 106 M -1 s-1 at pH 7.1. The protein does not require divalent cations in the active site for catalytic activity. BmulJ-04915 is the second enzyme from cog3618 of the amidohydrolase superfamily that does not require a divalent metal for catalytic activity. BmulJ-04915 is the first enzyme that has been shown to catalyze the hydrolysis of either l-fucono-1,4-lactone or l-fucono-1,5-lactone. The structures of the fuconolactonase and the fucose dehydrogenase were determined by X-ray diffraction methods.
De novo enantioselective syntheses of galacto-sugars and deoxy sugars via the iterative dihydroxylation of dienoate
Ahmed, Moinuddin Md.,Berry, Bryan P.,Hunter, Thomas J.,Tomcik, Dennis J.,O'Doherty, George A.
, p. 745 - 748 (2007/10/03)
(Chemical Equation Presented) An efficient route to various sugar lactones has been developed. Key to the overall transformation is the sequential osmium-catalyzed dihydroxylation of 2,4-dienoates. The simplest (one-step/racemic) example of this reaction occurs when the dihydroxylation is performed with aqueous NMO in MeOH. When the first dihydroxylation is performed using the AD-mix procedure, an enantioselective variant results. When a matched AD-mix procedure is used for the second dihydroxylation, an exceedingly diastereo- and enantioselective synthesis of galacto-1,4-lactone results.
