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.
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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
Original language English
Type of outcome Article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
WWW 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
Tags ne MU, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 28/2/2023 19:23.
Abstract
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
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