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塔斯曼尼亚欧文氏菌蔗糖酶表现出对(S)-1,2,4-丁三醇的对映体选择性。

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

机构信息

Bioorganic Chemistry and Bio-Crystallography Laboratory (B2Cl), Faculty of Science and Technology, Free University of Bolzano, Piazza Universita 5, 39100 Bolzano, Italy.

出版信息

Acta Crystallogr F Struct Biol Commun. 2022 Aug 1;78(Pt 8):289-296. doi: 10.1107/S2053230X2200680X. Epub 2022 Jul 26.

DOI:10.1107/S2053230X2200680X
PMID:35924596
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9350837/
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.

摘要

莱鲍迪苷酶是一种具有生物技术应用潜力的果糖基转移酶,因为它们可以用于酶法或化学-酶法合成与药物应用相关的非天然底物的糖苷。与(S)-1,2,4-丁三醇复合的塔斯曼尼亚欧文氏菌莱鲍迪苷酶的结构及其生化特性表明,在果糖基转移酶生物技术中,可能应用含有确定立体中心的短脂族部分的多元醇。结构信息表明,(S)-1,2,4-丁三醇模拟了天然底物。使用微量热泳动结合测定法评估了蛋白质对特定(S)-1,2,4-丁三醇对映体的偏好。此外,获得的结果和肠膜明串珠菌莱鲍迪苷酶和菊粉蔗糖酶的结构比较表明,来自革兰氏阳性和革兰氏阴性细菌的果糖基转移酶的果糖结合模式可能不同。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d755/9350837/eabf8a11fafe/f-78-00289-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d755/9350837/44959ec5d53b/f-78-00289-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d755/9350837/4a46b5b130c5/f-78-00289-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d755/9350837/f44fb22156ce/f-78-00289-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d755/9350837/eabf8a11fafe/f-78-00289-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d755/9350837/44959ec5d53b/f-78-00289-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d755/9350837/4a46b5b130c5/f-78-00289-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d755/9350837/f44fb22156ce/f-78-00289-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d755/9350837/eabf8a11fafe/f-78-00289-fig4.jpg

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Molecular insight into regioselectivity of transfructosylation catalyzed by GH68 levansucrase and β-fructofuranosidase.
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Crystal structure of a glycoside hydrolase family 68 β-fructosyltransferase from subsp. in complex with fructose.subsp. 中糖苷水解酶家族 68 型 β-呋喃果糖基转移酶与果糖复合物的晶体结构
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