Novel substrate specificities of two lacto-N-biosidases towards β-linked galacto-N-biose-containing oligosaccharides of globo H, Gb5, and GA1. (18th May 2015)
- Record Type:
- Journal Article
- Title:
- Novel substrate specificities of two lacto-N-biosidases towards β-linked galacto-N-biose-containing oligosaccharides of globo H, Gb5, and GA1. (18th May 2015)
- Main Title:
- Novel substrate specificities of two lacto-N-biosidases towards β-linked galacto-N-biose-containing oligosaccharides of globo H, Gb5, and GA1
- Authors:
- Gotoh, Aina
Katoh, Toshihiko
Sugiyama, Yuta
Kurihara, Shin
Honda, Yuji
Sakurama, Haruko
Kambe, Taiho
Ashida, Hisashi
Kitaoka, Motomitsu
Yamamoto, Kenji
Katayama, Takane - Abstract:
- Abstract: We describe the novel substrate specificities of two independently evolved lacto-N-biosidases (LnbX and LnbB) towards the sugar chains of globo- and ganglio-series glycosphingolipids. LnbX, a non-classified member of the glycoside hydrolase family, isolated from Bifidobacterium longum subsp. longum, was shown to liberate galacto-N-biose (GNB: Galβ1-3GalNAc) and 2′-fucosyl GNB (a type-4 trisaccharide) from Gb5 pentasaccharide and globo H hexasaccharide, respectively. LnbB, a member of the glycoside hydrolase family 20 isolated from Bifidobacterium bifidum, was shown to release GNB from Gb5 and GA1 oligosaccharides. This is the first report describing enzymatic release of β-linked GNB from natural substrates. These unique activities may play a role in modulating the microbial composition in the gut ecosystem, and may serve as new tools for elucidating the functions of sugar chains of glycosphingolipids. Graphical abstract: Highlights: Gut microbes have evolved selected enzymes to degrade host-derived glycans. We reveal novel substrate specificities of two non-homologous lacto-N-biosidases. LnbX, a non-classified GH member, acts on Gb5 and globo H oligosaccharides. LnbB, a member of GH20, acts on GA1 and Gb5 oligosaccharides. These enzymes will provide new tools for glycobiology.
- Is Part Of:
- Carbohydrate research. Volume 408(2015)
- Journal:
- Carbohydrate research
- Issue:
- Volume 408(2015)
- Issue Display:
- Volume 408, Issue 2015 (2015)
- Year:
- 2015
- Volume:
- 408
- Issue:
- 2015
- Issue Sort Value:
- 2015-0408-2015-0000
- Page Start:
- 18
- Page End:
- 24
- Publication Date:
- 2015-05-18
- Subjects:
- Lacto-N-biosidase -- β-Linked galacto-N-biose -- GA1 -- Gb5 -- Globo H
Carbohydrates -- Periodicals
Chemistry, Organic -- Periodicals
Biochemistry -- Periodicals
Carbohydrates -- Periodicals
Chimie organique -- Périodiques
Glucides -- Périodiques
Biochemistry
Carbohydrates
Chemistry, Organic
Periodicals
Electronic journals
507.78 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00086215 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.carres.2015.03.005 ↗
- Languages:
- English
- ISSNs:
- 0008-6215
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
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- British Library DSC - 3050.990500
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