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Difference between revisions of "Glycoside Hydrolase Family 139"

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* [[Author]]: [[User:Ana Luis|Ana Luis]]
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== Substrate specificities ==
 
== Substrate specificities ==
Glycoside hydrolases of GH139 family ([www.cazy.org/GH139.html CAZy]) display the novel a-2-O-methyl-L-fucosidase activity (EC…….). The enzyme BT0984 from Bacteroides thetaiotaomicron is the only member of this family that has been characterized. This exo-enzyme targets the a-2-O-methyl-L-fucose at chain B of the complex rhamnogalacturonan-II present in the plants cell wall. All of genes encoding family 139 members are found in bacteria.
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[[Glycoside hydrolases]] of family 139 family display α-2-''O''-methyl-L-fucosidase activity. They are exclusively bacterial in origin. The enzyme BT0984 from ''Bacteroides thetaiotaomicron'' is the only member of this family that has been characterized. This ''exo''-acting enzyme targets the 2-''O''-methyl-L-fucose-&alpha;-1,2-D-Galp linkage in chain B of the complex pectin rhamnogalacturonan-II <cite>Ndeh2017</cite>.
 
 
Content is to be added here.
 
 
 
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...)''
 
 
 
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 ==
Content is to be added here.
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The stereochemistry of the reaction catalyzed by GH139 members has not yet been reported.
  
 
== Catalytic Residues ==
 
== Catalytic Residues ==
Content is to be added here.
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Not known.
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==
Content is to be added here.
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No three-dimensional structure has been solved for this family.
  
 
== Family Firsts ==
 
== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
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;First stereochemistry determination: Unknown.
;First catalytic nucleophile identification: Content is to be added here.
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;First catalytic nucleophile identification: Unknown.
;First general acid/base residue identification: Content is to be added here.
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;First general acid/base residue identification: Unknown.
;First 3-D structure: Content is to be added here.
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;First 3-D structure: Unknown.
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
#Cantarel2009 pmid=18838391
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#Ndeh2017 pmid=28329766
#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. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
 
 
</biblio>
 
</biblio>
  
 
[[Category:Glycoside Hydrolase Families|GH139]]
 
[[Category:Glycoside Hydrolase Families|GH139]]

Latest revision as of 13:20, 18 December 2021

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Glycoside Hydrolase Family GH139
Clan none
Mechanism unknown
Active site residues not known
CAZy DB link
https://www.cazy.org/GH139.html


Substrate specificities

Glycoside hydrolases of family 139 family display α-2-O-methyl-L-fucosidase activity. They are exclusively bacterial in origin. The enzyme BT0984 from Bacteroides thetaiotaomicron is the only member of this family that has been characterized. This exo-acting enzyme targets the 2-O-methyl-L-fucose-α-1,2-D-Galp linkage in chain B of the complex pectin rhamnogalacturonan-II [1].

Kinetics and Mechanism

The stereochemistry of the reaction catalyzed by GH139 members has not yet been reported.

Catalytic Residues

Not known.

Three-dimensional structures

No three-dimensional structure has been solved for this family.

Family Firsts

First stereochemistry determination
Unknown.
First catalytic nucleophile identification
Unknown.
First general acid/base residue identification
Unknown.
First 3-D structure
Unknown.

References

  1. Ndeh D, Rogowski A, Cartmell A, Luis AS, Baslé A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neil MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, and Gilbert HJ. (2017). Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature. 2017;544(7648):65-70. DOI:10.1038/nature21725 | PubMed ID:28329766 [Ndeh2017]