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Literature summary for 2.4.1.101 extracted from

  • Zhong, X.; Cooley, C.; Seth, N.; Juo, Z.S.; Presman, E.; Resendes, N.; Kumar, R.; Allen, M.; Mosyak, L.; Stahl, M.; Somers, W.; Kriz, R.
    Engineering novel Lec1 glycosylation mutants in CHO-DUKX cells: molecular insights and effector modulation of N-acetylglucosaminyltransferase I (2012), Biotechnol. Bioeng., 109, 1723-1734.
    View publication on PubMed
Search for more literature for 2.4.1.101

Cloned(Commentary)

Cloned (Comment) Organism
expressed in CHO-DUKX-Lec1 cells Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
D291N inactive Oryctolagus cuniculus
more. deleting seven C-terminal amino acids of the enzyme reduces enzymatic activity by 40% Oryctolagus cuniculus
P138L inactive Oryctolagus cuniculus
R415K inactive Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus
-
 Oryctolagus cuniculus 5794
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required for activity Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Synonyms

Synonyms Comment Organism
GnTI
-
 Oryctolagus cuniculus
N-acetylglucosaminyltransferase I
-
 Oryctolagus cuniculus

General Information

General Information Comment Organism
malfunction modulating N-acetylglucosaminyltransferase I activity in cells can influence antibody effector functions Oryctolagus cuniculus