| Known Activities | heparan β-glucuronyltransferase (EC 2.4.1.225); xyloglucan β-galactosyltransferase (EC 2.4.1.-); heparan synthase (EC 2.4.1.-); arabinan α-L-arabinosyltransferase (EC 2.4.2.-). |
|---|---|
| Mechanism | Inverting |
| Note | The long animal heparan synthases are made of two domains. The N-terminal domain, which adds b-1,4-GlcA residues, belongs to family GT47 while the C-terminal domain, which adds a-1,4-GlcNAc residues, belongs to family GT64. The plant homologs, which have a single domain, display various specificities ranging from xyloglucan b-galactosyltransferase to a pectin b-glucuronyltransferase and arabinan a-L-arabinosyltransferase. |
| External resources | InterPro; PFAM; |
| Statistics | GenBank accession (599); Uniprot accession (229); |
Experimental characterization exclusively covers enzyme activities at present. If you are aware of any missing experimental characterization that should be mentioned here, we encourage you to send your comment and support of the experimental evidence, including an electronic copy or appropriate link to the support material (i.e., article(s), thesis, database, etc), to cazy@afmb.univ-mrs.fr.