An Alternative Synthesis of N-Acetyl-4-deoxyneuraminic Acid

Ooi, Hua Chee; Marcuccio, Sebastian M.; Jackson, W. R.

doi:10.1071/ch99117

Cited by 3 publications

(4 citation statements)

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“…B) . Conversely, 4‐deoxy sialic acid and 4‐oxo sialic acid are both capable of imine formation, but because they do not have a hydroxyl group at the C4 position, they cannot undergo retro‐aldol cleavage . The K i for the sialic acid alditols is 4.1 m m ; for 4‐deoxy sialic acid, it is 0.90 m m ; and for 4‐oxo sialic acid, it is 0.03 m m against C. perfringens N ‐acetylneuraminate lyase .…”

Section: Resultsmentioning

confidence: 99%

Structure and inhibition ofN‐acetylneuraminate lyase from methicillin‐resistantStaphylococcus aureus

et al. 2016

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N-Acetylneuraminate lyase is the first committed enzyme in the degradation of sialic acid by bacterial pathogens. In this study, we analyzed the kinetic parameters of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus (MRSA). We determined that the enzyme has a relatively high K of 3.2 mm, suggesting that flux through the catabolic pathway is likely to be controlled by this enzyme. Our data indicate that sialic acid alditol, a known inhibitor of N-acetylneuraminate lyase enzymes, is a stronger inhibitor of MRSA N-acetylneuraminate lyase than of Clostridium perfringens N-acetylneuraminate lyase. Our analysis of the crystal structure of ligand-free and 2R-sialic acid alditol-bound MRSA N-acetylneuraminate lyase suggests that subtle dynamic differences in solution and/or altered binding interactions within the active site may account for species-specific inhibition.

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Section: Resultsmentioning

confidence: 99%

Structure and inhibition ofN‐acetylneuraminate lyase from methicillin‐resistantStaphylococcus aureus

et al. 2016

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“…The correct structure assignment of lactone 10 was then additionally supported by its transformation to the saturated 1,7-lactone 12 , having an inverted classical 5 C 2 chair conformation (Scheme ). To this purpose, lactone 10 was submitted to a H 2 atmosphere in the presence of Pd on carbon, as a catalyst, in AcOEt to afford 12 as a white solid (Scheme , path A), which showed an identical structure to that obtained by a different route (Scheme , path B), consisting in the direct 1,7-lactonization of the saturated compound 13 …”

Section: Resultsmentioning

confidence: 99%

“…Starting from oxazoline 5 , we synthesized protected Ferrier derivatives 14a,b , 15a,b , and 16a,b . Then, the peracetylated compounds were converted to their methyl esters 17a,b , 18a,b , and 19a,b via a Zemplén reaction (Scheme ).…”

Section: Resultsmentioning

confidence: 99%

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Lactonization Method To Assign the Anomeric Configuration of the 3,4-Unsaturated Congeners of N-Acetylneuraminic Acid

et al. 2019

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Assigning the correct configuration at C2 in sialosides is a standing problem because of the absence of an anomeric hydrogen. All different empirical rules that have been proposed over the years lack general applicability. In particular, the correct configuration of several 3,4-unsaturated derivatives of N-acetylneuraminic acid (Neu5Ac), which have been recently shown to be novel sialidase/neuraminidase inhibitors, could only be tentatively assigned by similarity with the reported 3,4unsaturated 2O-methyl sialosides. In this work, we overcome this problem as we devised a rapid synthetic method to unequivocally resolve the anomeric configuration of the 3,4-unsaturated Neu5Ac derivatives through the synthesis of the corresponding unreported unsaturated 1,7-lactones. Moreover, we discovered a diagnostic 13 C nuclear magnetic resonance signal that allows the formulation of a new empirical rule for the direct assignment of the C2 stereochemistry of these molecules, even when only one of the two C2 epimers is available. Article pubs.acs.org/joc

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Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme

Barbosa¹,

Smith²,

DeGori³

et al. 2000

Journal of Molecular Biology

117

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An Alternative Synthesis of N-Acetyl-4-deoxyneuraminic Acid

Cited by 3 publications

References 0 publications

Structure and inhibition ofN‐acetylneuraminate lyase from methicillin‐resistantStaphylococcus aureus

Structure and inhibition ofN‐acetylneuraminate lyase from methicillin‐resistantStaphylococcus aureus

Lactonization Method To Assign the Anomeric Configuration of the 3,4-Unsaturated Congeners of N-Acetylneuraminic Acid

Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme

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