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Literature summary for 2.4.1.41 extracted from

  • Yoshimura, Y.; Nudelman, A.S.; Levery, S.B.; Wandall, H.H.; Bennett, E.P.; Hindsgaul, O.; Clausen, H.; Nishimura, S.
    Elucidation of the sugar recognition ability of the lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3 by using unnatural glycopeptide substrates (2012), Glycobiology, 22, 429-438.
    View publication on PubMed
Search for more literature for 2.4.1.41

Cloned(Commentary)

Cloned (Comment) Organism
His tagged truncated protein expressed in High Five cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
D519H inactivated lectin domain Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ion exchange chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-alpha-D-galactosamine + (glycosylated GTTPSPVPTTSTTSAP) natural-type (alpha-GalNAc-O-Thr) and unnatural-type (beta-GalNAc-O-Thr, alpha-Fuc-O-Thr and beta-GlcNAc-O-Thr) glycosylated Homo sapiens UDP + ?
-
 ?
UDP-N-acetyl-alpha-D-galactosamine + GTTPSPVPTTSTTSAP
-
 Homo sapiens UDP + ?
-
 ?

Synonyms

Synonyms Comment Organism
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
-
 Homo sapiens
uridine diphosphate-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function the lectin domain strictly recognizes GalNAc on the substrate and this specificity controls the glycosylation pathway Homo sapiens