Difference between revisions of "Glycoside Hydrolase Family 139"

Revision as of 13:41, 11 February 2018

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.

Author: ^^^Ana Luis^^^
Responsible Curator: ^^^Harry Gilbert^^^

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

Substrate specificities

Glycoside hydrolases of GH139 family (CAZy) display the novel α-2-O-methyl-L-fucosidase activity. The enzyme BT0984 from Bacteroides thetaiotaomicron is the only member of this family that has been characterized. This exo-enzyme targets the α-2-O-methyl-L-fucose at chain B of the complex pectin rhamnogalacturonan-II [1]. All of genes encoding family 139 members are found in bacteria.

Kinetics and Mechanism

The stereochemistry of the reaction catalyzed by GH129 members has not yet been studied.

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

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]

@@ Line 29: / Line 29: @@
 == 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.
+Glycoside hydrolases of GH139 family ([http://www.cazy.org/GH139.html CAZy]) display the novel α-2-O-methyl-L-fucosidase activity. The enzyme BT0984 from ''Bacteroides thetaiotaomicron'' is the only member of this family that has been characterized. This exo-enzyme targets the α-2-O-methyl-L-fucose at chain B of the complex pectin rhamnogalacturonan-II <cite>Ndeh2017</cite>. All of genes encoding family 139 members are found in bacteria.
-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 ==
-Content is to be added here.
+The stereochemistry of the reaction catalyzed by GH129 members has not yet been studied.
 == Catalytic Residues ==
-Content is to be added here.
+Not known.
 == Three-dimensional structures ==
-Content is to be added here.
+No three-dimensional structure has been solved for this family.
 == Family Firsts ==
-;First stereochemistry determination: Content is to be added here.
+;First stereochemistry determination: Unknown.
-;First catalytic nucleophile identification: Content is to be added here.
+;First catalytic nucleophile identification: Unknown.
-;First general acid/base residue identification: Content is to be added here.
+;First general acid/base residue identification: Unknown.
-;First 3-D structure: Content is to be added here.
+;First 3-D structure: Unknown.
 == References ==
 <biblio>
-#Cantarel2009 pmid=18838391
+#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>
 [[Category:Glycoside Hydrolase Families|GH139]]