| Activities in Family | DTDP-L-Rha: α-L-rhamnosyltransferase (EC 2.4.1.-); |
|---|---|
| Mechanism | Inverting |
| Note | Lassak et al. identified EarP as EF-P arginine R32 specific rhamnosyl transferase in Shewanella oneidensis using dTDP-b-L-rhamnose as donor substrate (PMID=25686373). The results of this study were subsequently confirmed for Pseudomonas aeruginosa (PMID=26060278), Pseudomonas putida (PMID=28951478) and Neisseria meningitidis (PMID=26840407). In 2016, it has been shown for S. oneidensis (PMID=28451135) and P. aeruginosa (PMID=28451332) that the enzyme is an inverting glycosyltransferase, thus mediating the formation of an a-L-rhamnosidic linkage. A structural basis for the arginine glycosylation reaction was provided by Krafczyk, Macosek and coworkers by having solved the crystal structure of the GT-B folding EarP from P. putida and an accompanying biochemical analysis of the enzyme (PMID=28951478). |
| Statistics | GenBank accession (3950); Uniprot accession (4); PDB accession (12); 3D entries (4); cryst (0) |
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