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Glycoside Hydrolase Family 151
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|Glycoside Hydrolase Family GH151|
|Active site residues||Known|
|CAZy DB link|
Members of GH151 are bacterial enzymes presenting α-L-fucosidase activity (EC 22.214.171.124) [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) . 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 . No activity was observed on fucosylated xyloglucan .
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 . Sequence homology to GH42 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 .
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 or CNP-α-L-Fuc as donor substrate [2, 3, 4], a retaining mechanism has been inferred.
In the α-L-fucosidase isoenzyme 2 from Paenibacillus thiaminolyticus, Glu235 was assigned as catalytic acid/base and Asp154 as catalytic nucleophile following a combination of mutational, structural, docking, and QM/MM studies . Initially, both Asp9 and Asp154 were investigated as putative nucleophiles. However, docking studies combined with the fact that the variant D9N performed well in transglycosylation  indicated that the role of Asp9 is in substrate binding .
The first solved structure in GH151 was that of α-L-fucosidase isoenzyme 2 from Paenibacillus thiaminolyticus. It revealed a tetrameric structure with active site complementation by His503 .
- First stereochemistry determination
- Not yet identified.
- First catalytic nucleophile identification
- Asp154 in α-L-fucosidase isoenzyme 2 from Paenibacillus thiaminolyticus .
- First general acid/base residue identification
- Glu235 in α-L-fucosidase isoenzyme 2 from Paenibacillus thiaminolyticus .
- First 3-D structure
- The 3-D structure of α-L-fucosidase isoenzyme 2 from Paenibacillus thiaminolyticus .
- 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 |
- 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 |
- 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 |
- Teze D, Zhao J, Wiemann M, Kazi ZGA, Lupo R, Zeuner B, Vuillemin M, Rønne ME, Carlström G, Duus JØ, Sanejouand YH, O'Donohue MJ, Nordberg Karlsson E, Fauré R, Stålbrand H, and Svensson B. (2021). Rational Enzyme Design without Structural Knowledge: A Sequence-Based Approach for Efficient Generation of Transglycosylases. Chemistry. 2021;27(40):10323-10334. DOI:10.1002/chem.202100110 |
- Koval'ová T, Kovaľ T, Stránský J, Kolenko P, Dušková J, Švecová L, Vodičková P, Spiwok V, Benešová E, Lipovová P, and Dohnálek J. (2022). The first structure-function study of GH151 α-l-fucosidase uncovers new oligomerization pattern, active site complementation, and selective substrate specificity. FEBS J. 2022;289(16):4998-5020. DOI:10.1111/febs.16387 |