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
http://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

Not yet identified.

First catalytic nucleophile identification

Not yet identified.

First general acid/base residue identification

Not yet identified.

First 3-D structure

Not yet identified.

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 |