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 a Stefano BENINI

Základní údaje

Originální název

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

Autoři

POLSINELLI, Ivan, Marco SALOMONE-STAGNI a Stefano BENINI

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 0.900

Kód RIV

RIV/00216224:14740/22:00128778

Organizační jednotka

Středoevropský technologický institut

DOI

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

UT WoS

000837899700001

Klíčová slova anglicky

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

Štítky

ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 2. 2023 19:23, Mgr. Pavla Foltynová, Ph.D.

Anotace

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

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

POLSINELLI, Ivan, Marco SALOMONE-STAGNI a 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, roč. 78, AUG, s. 289-296. ISSN 2053-230X. Dostupné z: 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 a 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, roč.~78, AUG, s.~289-296. ISSN~2053-230X. Dostupné z: https://dx.doi.org/10.1107/S2053230X2200680X.

Podrobný výpis o publikaci