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Difference between revisions of "Glycoside Hydrolase Family 151"

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Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''
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Members of GH151 have α-L-fucosidase activity <cite>Sela2012 Benesova2015 Lezyk2016</cite>.
 
 
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
 
  
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
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== References ==
 
== References ==
 
<biblio>
 
<biblio>
#Cantarel2009 pmid=18838391
 
  
 
#Lezyk2016 pmid=26800369
 
#Lezyk2016 pmid=26800369
 
#Sela2012 pmid=22138995
 
#Sela2012 pmid=22138995
 
 
#Benesova2015 pmid=26013545
 
#Benesova2015 pmid=26013545
  
 
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [https://doi.org/10.1042/BIO03004026 Download PDF version].
 
  
 
</biblio>
 
</biblio>

Revision as of 02:03, 15 May 2020

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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.


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

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Members of GH151 have α-L-fucosidase activity [1, 2, 3].

Kinetics and Mechanism

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Catalytic Residues

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Three-dimensional structures

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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 | PubMed ID:22138995 [Sela2012]
  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 | PubMed ID:26013545 [Benesova2015]
  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 | PubMed ID:26800369 [Lezyk2016]

All Medline abstracts: PubMed