Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 14, Issue 1, Pages 105-112Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5ob02037a
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Funding
- BBSRC
- EPSRC [EP/K039202/1]
- AstraZeneca
- Biotechnology and Biological Sciences Research Council [1087797, BB/L015056/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/K039202/1] Funding Source: researchfish
- BBSRC [BB/L015056/1] Funding Source: UKRI
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The catalysis of reactions involving fluoropyruvate as donor by N-acetyl neuraminic acid lyase (NAL) variants was investigated. Under kinetic control, the wild-type enzyme catalysed the reaction between fluoropyruvate and N-acetyl mannosamine to give a 90 : 10 ratio of the (3R, 4R)-and (3S, 4R)-configured products; after extended reaction times, equilibration occurred to give a 30 : 70 mixture of these products. The efficiency and stereoselectivity of reactions of a range of substrates catalysed by the E192N, E192N/T167V/S208V and E192N/T167G NAL variants were also studied. Using fluoropyruvate and (2R, 3S)- or (2S, 3R)-2,3-dihydroxy-4-oxo-N,N-dipropylbutanamide as substrates, it was possible to obtain three of the four possible diastereomeric products; for each product, the ratio of anomeric and pyranose/furanose forms was determined. The crystal structure of S. aureus NAL in complex with fluoropyruvate was determined, assisting rationalisation of the stereochemical outcome of C-C bond formation.
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