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Difference between revisions of "Glycoside Hydrolase Family 151"
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Revision as of 01:14, 15 May 2020
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Authors: ^^^Casper Wilkens^^^, ^^^David Teze^^^, and ^^^Birgitte Zeuner^^^
- Responsible Curator: ^^^Birgitte Zeuner^^^
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
Content is to be added here.
Members of GH151 have α-L-fucosidase activity [1, 2, 3].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Content is to be added here.
- First catalytic nucleophile identification
- Content is to be added here.
- First general acid/base residue identification
- Content is to be added here.
- First 3-D structure
- Content is to be added here.
References
- 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 |