Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.68 extracted from

  • Li, C.; Zhu, S.; Ma, C.; Wang, L.X.
    Designer alpha1,6-fucosidase mutants enable direct core fucosylation of intact N-glycopeptides and N-glycoproteins (2017), J. Am. Chem. Soc., 139, 15074-15087 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
synthesis mutants of the general acid/base residue E274, including E274A, E274S, and E274G, act as efficient glycoligases able to fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins by using alpha-fucosyl fluoride as a simple donor substrate. The alpha-1,6-fucosidase mutants can introduce an alpha1,6-fucose moiety specifically at the Asn-linked GlcNAc moiety to GlcNAc-peptide, and also to high-mannose and complex type N-glycans in the context of N-glycopeptides, N-glycoproteins, and intact antibodies Lacticaseibacillus casei

Protein Variants

Protein Variants Comment Organism
D200A mutation at the nucleophilic residue, does not provide a typical glycosynthase activity Lacticaseibacillus casei
E274A mutation at the general acid/base residue, mutant acts as efficient glycoligase able to fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins Lacticaseibacillus casei
E274G mutation at the general acid/base residue, mutant acts as efficient glycoligase able to fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins Lacticaseibacillus casei
E274S mutation at the general acid/base residue, mutant acts as efficient glycoligase able to fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins Lacticaseibacillus casei

Organism

Organism UniProt Comment Textmining
Lacticaseibacillus casei
-
-
-
Lacticaseibacillus casei W56
-
-
-

Synonyms

Synonyms Comment Organism
alfC
-
Lacticaseibacillus casei
BN194_28780
-
Lacticaseibacillus casei