Difference between revisions of "Glycoside Hydrolase Family 168"

Revision as of 12:19, 18 June 2023

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Glycoside Hydrolase Family GH168
Clan	GH-x
Mechanism	retaining
Active site residues	not known
CAZy DB link
http://www.cazy.org/GH168.html

Substrate specificities

Members of GH168 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun168A from a marine bacterium Wenyingzhuangia funcanilytica CZ1127^T, specifically hydrolyzes the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber Isostichopus badionotus in a random endo-acting manner. Meanwhile, five homologues of Fun168A display activities toward sulfated fucan from Isostichopus badionotus [1].

Figure 1. The phylogenetic tree of GH168 homologues. Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.

Kinetics and Mechanism

As mentioned in the report, Fun168A exhibited transglycosylating activity with glycerin, methanol, and L-fucose as acceptors. The transglycosylating activity of Fun168A implied its retaining mechanism in catalysis [1].

Catalytic Residues

Multiple sequence alignments of GH168 homologues showed that D206 and E264 in Fun168A were strictly conserved in all sequences. Two single-site mutants D206E and E264Q were established, expressed and identified in the report. These two mutants were all inactive on Ib-FUC, indicating that D206 and E264 were critical for the activity of Fun168A [1].

Figure 2. Multiple sequence alignments of residues in GH168 homologues. The strictly conserved residues in all sequences were indicated with black triangles.

Three-dimensional structures

No three-dimensional structure has been solved in this glycoside hydrolase family at present.

Family Firsts

First stereochemistry determination: Not yet identified.
First catalytic nucleophile identification: Not yet identified.
First general acid/base residue identification: Not yet identified.
First 3-D structure: Not yet identified.

References

Shen J, Chang Y, Zhang Y, Mei X, and Xue C. (2020). Discovery and Characterization of an Endo-1,3-Fucanase From Marine Bacterium Wenyingzhuangia fucanilytica: A Novel Glycoside Hydrolase Family. Front Microbiol. 2020;11:1674. DOI:10.3389/fmicb.2020.01674 | PubMed ID:32849348 [Shen2020]

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 == Substrate specificities ==
-Members of [[GH168|glycoside hydrolase family 168]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun168A from a marine bacterium ''Wenyingzhuangia funcanilytica'' CZ1127<sup>T</sup>, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a random endo-acting manner. Meanwhile, five homologues of Fun168A display activities toward sulfated fucan from ''Isostichopus badionotus'', namely WP_081987558.1, WP_068826447.1, WP_068826442.1, OHE80969.1 and WP_083194720.1 <cite>Shen2020</cite>.
+Members of GH168 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun168A from a marine bacterium ''Wenyingzhuangia funcanilytica'' CZ1127<sup>T</sup>, specifically hydrolyzes the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a random endo-acting manner. Meanwhile, [http://www.cazy.org/GH168_characterized.html five homologues of Fun168A display activities toward sulfated fucan] from ''Isostichopus badionotus'' <cite>Shen2020</cite>.
 [[File:Tree of GH168.png|thumb|'''Figure 1. The phylogenetic tree of GH168 homologues.''' Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.]]