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Int. J. Mol. Sci. 2015, 16(6), 13714-13728; doi:10.3390/ijms160613714

Enzymatic Synthesis of Galactosylated Serine/Threonine Derivatives by β-Galactosidase from Escherichia coli

1
Department of Food Science and Agricultural Chemistry, McGill University, 21,111 Lakeshore, Ste Anne de Bellevue, QC H9X-3V9, Canada
2
INSERM UMR_S 1134, Dynamique des Structures et Interactions des Macromolécules Biologiques (DSIMB), University Paris Diderot, Sorbonne Paris Cité, INTS, Laboratory of excellence, GR-Ex, 6, rue Alexandre Cabanel, 75739 Paris Cedex 15, France
*
Author to whom correspondence should be addressed.
Academic Editors: Patricia Berninsone and Joe Tiralongo
Received: 14 May 2015 / Accepted: 11 June 2015 / Published: 15 June 2015
(This article belongs to the Special Issue Glycosylation and Glycoproteins)
View Full-Text   |   Download PDF [1403 KB, uploaded 15 June 2015]   |  

Abstract

The transgalactosylations of serine/threonine derivatives were investigated using β-galactosidase from Escherichia coli as biocatalyst. Using ortho-nitrophenyl-β-D-galactoside as donor, the highest bioconversion yield of transgalactosylated N-carboxy benzyl L-serine benzyl ester (23.2%) was achieved in heptane:buffer medium (70:30), whereas with the lactose, the highest bioconversion yield (3.94%) was obtained in the buffer reaction system. The structures of most abundant galactosylated serine products were characterized by MS/MS. The molecular docking simulation revealed that the binding of serine/threonine derivatives to the enzyme’s active site was stronger (−4.6~−7.9 kcal/mol) than that of the natural acceptor, glucose, and mainly occurred through interactions with aromatic residues. For N-tert-butoxycarbonyl serine methyl ester (6.8%) and N-carboxybenzyl serine benzyl ester (3.4%), their binding affinities and the distances between their hydroxyl side chain and the 1′-OH group of galactose moiety were in good accordance with the quantified bioconversion yields. Despite its lower predicted bioconversion yield, the high experimental bioconversion yield obtained with N-carboxybenzyl serine methyl ester (23.2%) demonstrated the importance of the thermodynamically-driven nature of the transgalactosylation reaction. View Full-Text
Keywords: β-galactosidase; transgalactosylation; serine/threonine derivatives; molecular docking; binding affinities; galactosyl acceptor β-galactosidase; transgalactosylation; serine/threonine derivatives; molecular docking; binding affinities; galactosyl acceptor
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MDPI and ACS Style

Seo, S.; Rebehmed, J.; de Brevern, A.G.; Karboune, S. Enzymatic Synthesis of Galactosylated Serine/Threonine Derivatives by β-Galactosidase from Escherichia coli. Int. J. Mol. Sci. 2015, 16, 13714-13728.

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