2014
DOI: 10.1002/cbic.201300699
|View full text |Cite
|
Sign up to set email alerts
|

Characterization of a Galactosynthase Derived from Bacillus circulans β‐Galactosidase: Facile Synthesis of D‐Lacto‐ and D‐Galacto‐N‐bioside

Abstract: Glycosynthases-retaining glycosidases mutated at their catalytic nucleophile-catalyze the formation of glycosidic bonds from glycosyl fluorides as donor sugars and various glycosides as acceptor sugars. Here the first glycosynthase derived from a family 35 β-galactosidase is described. The Glu→Gly mutant of BgaC from Bacillus circulans (BgaC-E233G) catalyzed regioselective galactosylation at the 3-position of the sugar acceptors with α-galactosyl fluoride as the donor. Transfer to 4-nitophenyl α-D-N-acetyl-glu… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
2

Citation Types

0
13
0

Year Published

2014
2014
2024
2024

Publication Types

Select...
5
1

Relationship

0
6

Authors

Journals

citations
Cited by 14 publications
(13 citation statements)
references
References 41 publications
0
13
0
Order By: Relevance
“…Interestingly, K M,app and v max could not be determined for the novel acceptor substrate 1 as the fitted curve did not show saturation within the investigated substrate concentration range. In a previous study, K M values between 0.71 mM and 0.41 mM were reported for the arylglycosides pNP-αGlcNAc and pNP-αGalNAc, respectively [31]. The difference in K M values may be due to a generally higher affinity of the wild type glycosidase for aryl-substituted glycosides compared to unmodified acceptor substrates [38].…”
Section: Kinetic Analysis Of the Synthesis Reaction Using The Glycosynthase Bgac/glu233glymentioning
confidence: 93%
See 3 more Smart Citations
“…Interestingly, K M,app and v max could not be determined for the novel acceptor substrate 1 as the fitted curve did not show saturation within the investigated substrate concentration range. In a previous study, K M values between 0.71 mM and 0.41 mM were reported for the arylglycosides pNP-αGlcNAc and pNP-αGalNAc, respectively [31]. The difference in K M values may be due to a generally higher affinity of the wild type glycosidase for aryl-substituted glycosides compared to unmodified acceptor substrates [38].…”
Section: Kinetic Analysis Of the Synthesis Reaction Using The Glycosynthase Bgac/glu233glymentioning
confidence: 93%
“…The high product yield results from a lack in product hydrolysis [32]. In addition, BgaC/Glu233Gly, unlike other reported glycosynthase mutants [37], does not accept β1,3-linked galactosides as acceptor substrates [31]. Further reduction in yield due to the formation of GAOS is therefore prevented.…”
Section: Synthesis Of Tf-antigen-eg3-azide (6)mentioning
confidence: 93%
See 2 more Smart Citations
“…A β-galactosidase from T. thermophilus, TtbGly, was converted to a glycosynthase and applied in the stereoselective β-galactosylation of 2-amino-3- thiazolylpropan-1,3-diol, a precursor for sphingosine synthesis. 457 Recently, another galactosynthase was generated from B. circulans (BgaC E233G ) and was found to selectively catalyze the formation of a β1,3-galactosyl linkage in LacNAc, galacto-N-biose analogues, 458,459 and poly-LacNAc oligomers (in combination with glycosyltransferases). 460 A glycosynthase was engineered from endoglycoceramidase II (EGCase II, Rhodococcus) and used for glycosylation of ceramide precursors.…”
Section: Chemoenzymatic Synthesis Using Glycosidases and Glycosynthasesmentioning
confidence: 99%