Erwinia tasmaniensis levansucrase shows enantiomer selection
for (S)-1,2,4-butanetriol

J 2022

Erwinia tasmaniensis levansucrase shows enantiomer selection for (S)-1,2,4-butanetriol

POLSINELLI, Ivan, Marco SALOMONE-STAGNI and Stefano BENINI

Basic information

Original name

Erwinia tasmaniensis levansucrase shows enantiomer selection for (S)-1,2,4-butanetriol

Authors

POLSINELLI, Ivan, Marco SALOMONE-STAGNI and Stefano BENINI

Edition

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, CHESTER, INT UNION CRYSTALLOGRAPHY, 2022, 2053-230X

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 0.900

RIV identification code

RIV/00216224:14740/22:00128778

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1107/S2053230X2200680X

UT WoS

000837899700001

Keywords in English

fructosyltransferases; transfructosylation; glycosyl hydrolases; microscale thermophoresis; binding assays; levansucrases; Erwinia tasmaniensis

Abstract

V originále

Levansucrases are biotechnologically interesting fructosyltransferases due to their potential use in the enzymatic or chemo-enzymatic synthesis of glycosides of non-natural substrates relevant to pharmaceutical applications. The structure of Erwinia tasmaniensis levansucrase in complex with (S)-1,2,4-butanetriol and its biochemical characterization suggests the possible application of short aliphatic moieties containing polyols with defined stereocentres in fructosylation biotechnology. The structural information revealed that (S)-1,2,4-butanetriol mimics the natural substrate. The preference of the protein towards a specific 1,2,4-butanetriol enantiomer was assessed using microscale thermophoresis binding assays. Furthermore, the results obtained and the structural comparison of levansucrases and inulosucrases suggest that the fructose binding modes could differ in fructosyltransferases from Gram-positive and Gram-negative bacteria. Keywords

Links

90127, large research infrastructures

Name: CIISB II

Citovat

POLSINELLI, Ivan, Marco SALOMONE-STAGNI and Stefano BENINI. Erwinia tasmaniensis levansucrase shows enantiomer selection for (S)-1,2,4-butanetriol. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS. CHESTER: INT UNION CRYSTALLOGRAPHY, 2022, vol. 78, AUG, p. 289-296. ISSN 2053-230X. Available from: https://dx.doi.org/10.1107/S2053230X2200680X.

@article{2262565,
   author = {Polsinelli, Ivan and SalomoneandStagni, Marco and Benini, Stefano},
   article_location = {CHESTER},
   article_number = {AUG},
   doi = {http://dx.doi.org/10.1107/S2053230X2200680X},
   keywords = {fructosyltransferases; transfructosylation; glycosyl hydrolases; microscale thermophoresis; binding assays; levansucrases; Erwinia tasmaniensis},
   language = {eng},
   issn = {2053-230X},
   journal = {ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS},
   title = {Erwinia tasmaniensis levansucrase shows enantiomer selection for (S)-1,2,4-butanetriol},
   url = {https://scripts.iucr.org/cgi-bin/paper?S2053230X2200680X},
   volume = {78},
   year = {2022}
}

TY  - JOUR
ID  - 2262565
AU  - Polsinelli, Ivan - Salomone-Stagni, Marco - Benini, Stefano
PY  - 2022
TI  - Erwinia tasmaniensis levansucrase shows enantiomer selection for (S)-1,2,4-butanetriol
JF  - ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
VL  - 78
IS  - AUG
SP  - 289-296
EP  - 289-296
PB  - INT UNION CRYSTALLOGRAPHY
SN  - 2053230X
KW  - fructosyltransferases
KW  - transfructosylation
KW  - glycosyl hydrolases
KW  - microscale thermophoresis
KW  - binding assays
KW  - levansucrases
KW  - Erwinia tasmaniensis
UR  - https://scripts.iucr.org/cgi-bin/paper?S2053230X2200680X
N2  - Levansucrases are biotechnologically interesting fructosyltransferases due to their potential use in the enzymatic or chemo-enzymatic synthesis of glycosides of non-natural substrates relevant to pharmaceutical applications. The structure of Erwinia tasmaniensis levansucrase in complex with (S)-1,2,4-butanetriol and its biochemical characterization suggests the possible application of short aliphatic moieties containing polyols with defined stereocentres in fructosylation biotechnology. The structural information revealed that (S)-1,2,4-butanetriol mimics the natural substrate. The preference of the protein towards a specific 1,2,4-butanetriol enantiomer was assessed using microscale thermophoresis binding assays. Furthermore, the results obtained and the structural comparison of levansucrases and inulosucrases suggest that the fructose binding modes could differ in fructosyltransferases from Gram-positive and Gram-negative bacteria. Keywords
ER  -

POLSINELLI, Ivan, Marco SALOMONE-STAGNI and Stefano BENINI. Erwinia tasmaniensis levansucrase shows enantiomer selection for (S)-1,2,4-butanetriol. \textit{ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS}. CHESTER: INT UNION CRYSTALLOGRAPHY, 2022, vol.~78, AUG, p.~289-296. ISSN~2053-230X. Available from: https://dx.doi.org/10.1107/S2053230X2200680X.

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