Glycoside Hydrolase Family 151

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• Author: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^
• Responsible Curator: ^^^Birgitte Zeuner^^^

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Glycoside Hydrolase Family GH151
Clan	None
Mechanism	Retaining (inferred)
Active site residues	Not known
CAZy DB link
https://www.cazy.org/GH151.html

Substrate specificities

Members of GH151 have α-L-fucosidase activity (EC 3.2.1.51) [1, 2, 3]. Activity has been observed on 4-nitrophenyl-α-L-fucopyranoside (pNP-α-L-Fuc) [2, 3] and on 2-chloro-4-nitrophenyl-α-L-fucopyranoside (CNP-α-L-Fuc) [1]. GH151 α-L-fucosidases are reportedly unable to catalyze hydrolysis of human milk oligosaccharide structures 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL) [1, 3], but slight activity has been observed on the blood group H antigen disaccharide Fuc-α-1,2-Gal [1]. No activity was observed on fucosylated xyloglucan [3].

The first characterized members of GH151 were perceived as members of GH29 due to their α-L-fucosidase activity [1, 3]. However, phylogenetic analysis and sequence alignment revealed poor homology to GH29 [1, 3]. Based on the low sequence similarity to GH29, it was suggested that a new GH family be created [2]. Sequence homology to β-galactosidase trimerization domains has been reported [1, 3]. Consequently, one GH151 α-L-fucosidase was tested for activity on pNP-β-D-Gal, pNP-β-D-Glc, and pNP-β-D-Lac, but none was observed [3].

Kinetics and Mechanism

The catalytic mechanism of GH151 has not been determined, but based on reports that two members of GH151 can catalyze transglycosylation using pNP-α-L-Fuc as donor substrate [2, 3], a retaining mechanism has been inferred.

Catalytic Residues

The catalytic residues of GH151 are unknown.

Three-dimensional structures

No three-dimensional structures have been solved for GH151.

Family Firsts

First stereochemistry determination

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First catalytic nucleophile identification

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First general acid/base residue identification

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First 3-D structure

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References

1. Sela DA, Garrido D, Lerno L, Wu S, Tan K, Eom HJ, Joachimiak A, Lebrilla CB, and Mills DA. (2012). Bifidobacterium longum subsp. infantis ATCC 15697 α-fucosidases are active on fucosylated human milk oligosaccharides. Appl Environ Microbiol. 2012;78(3):795-803. DOI:10.1128/AEM.06762-11 |
2. Benešová E, Lipovová P, Krejzová J, Kovaľová T, Buchtová P, Spiwok V, and Králová B. (2015). Alpha-L-fucosidase isoenzyme iso2 from Paenibacillus thiaminolyticus. BMC Biotechnol. 2015;15:36. DOI:10.1186/s12896-015-0160-x |
3. Lezyk M, Jers C, Kjaerulff L, Gotfredsen CH, Mikkelsen MD, and Mikkelsen JD. (2016). Novel α-L-Fucosidases from a Soil Metagenome for Production of Fucosylated Human Milk Oligosaccharides. PLoS One. 2016;11(1):e0147438. DOI:10.1371/journal.pone.0147438 |