Mechanism | Unknown e |
---|---|
3D Structure Status | parallel β-helix |
Catalytic Nucleophile/Base | Asp |
Catalytic Proton Donor | Asp |
Note | Created after Ndeh et al., Nature (2017) 544:65-70 (PMID=28329766) who have shown the a-L-fucosidase activity of the B. thetaiotaomicron enzyme. The xylanase activity of the (Rumini)clostridium thermocellum enzyme was shown by Heinze et al. (PMID=28894250) |
External resources | CAZypedia; |
Statistics | GenBank accession (1565); Uniprot accession (2); PDB accession (1); 3D entries (1); cryst (0) |
Activity Id | EC# | Activity Name | Residue -2 | Bond -1 | Residue -1 | Reacting Bond | Residue +1 | Bond +1 | Residue +2 | Reactant |
H7 | 3.2.1.8 | xylan endo-b-1,4-xylosidase | bDXylp | 1,4 | bDXylp | 1,4 | bDXylp | 1,4 | bDXylp | H2O |
H37 | 3.2.1.51 | a-L-fucosidase | [aLFucp | 1,X | alcohol | H2O | ||||
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