English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Characterization of five marine family 29 glycoside hydrolases reveals an alpha-L-fucosidase targeting specifically Fuc(alpha 1,4)GlcNAc

Schultz-Johansen, M., Stougaard, P., Svensson, B., & Teze, D. (2022). Characterization of five marine family 29 glycoside hydrolases reveals an alpha-L-fucosidase targeting specifically Fuc(alpha 1,4)GlcNAc. GLYCOBIOLOGY, 32(6), 529-539. doi:10.1093/glycob/cwab132.

Item is

Files

show Files
hide Files
:
cwab132-3.pdf (Publisher version), 2MB
Name:
cwab132-3.pdf
Description:
-
OA-Status:
Not specified
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Schultz-Johansen, Mikkel1, Author           
Stougaard, Peter2, Author
Svensson, Birte2, Author
Teze, David2, Author
Affiliations:
1Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481692              
2external, ou_persistent22              

Content

show
hide
Free keywords: -
 Abstract: L-Fucose is the most widely distributed L-hexose in marine and terrestrial environments and presents a variety of functional roles. L-Fucose is the major monosaccharide in the polysaccharide fucoidan from cell walls of brown algae and is found in human milk oligosaccharides (HMOs) and the Lewis blood group system, where it is important in cell signaling and immune response stimulation. Removal of fucose from these biomolecules is catalyzed by fucosidases belonging to different carbohydrate-active enzyme (CAZy) families. Fucosidases of glycoside hydrolase family 29 (GH29) release alpha-L-fucose from non-reducing ends of glycans and display activities targeting different substrate compositions and linkage types. While several GH29 fucosidases from terrestrial environments have been characterized, much less is known about marine members of GH29 and their substrate specificities, as only four marine GH29 enzymes were previously characterized. Here, five GH29 fucosidases originating from an uncultured fucoidandegrading marine bacterium (Paraglaciecola sp.) were cloned and produced recombinantly in Escherichia coli. All five enzymes (Fp231, Fp239, Fp240, Fp251 and Fp284) hydrolyzed the synthetic substrate CNP-alpha-L-fucose. Assayed against up to 17 fucose-containing oligosaccharides, Fp239 showed activity against the Lewis Y antigen, 2'- and 3-fucosyllactose, while Fp284 degraded 2'-fucosyllactose and Fuc(alpha 1,6)GlcNAc. Furthermore, Fp231 displayed strict specificity against Fuc(alpha 1,4)GlcNAc, a previously unreported specificity in GH29. Fp231 is a monomeric enzyme with pH and temperature optima at pH 5.6-6.0 and 25 degrees C, hydrolyzing Fuc(alpha 1,4)GlcNAc with k(cat) = 1.3 s(-1) and K-m = 660 mu M. Altogether, the findings extend our knowledge about GH29 family members from the marine environment, which are so far largely unexplored.

Details

show
hide
Language(s): eng - English
 Dates: 2022-01-052022
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000784741300001
DOI: 10.1093/glycob/cwab132
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: GLYCOBIOLOGY
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 32 (6) Sequence Number: - Start / End Page: 529 - 539 Identifier: ISSN: 0959-6658