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Literature summary for 2.4.1.101 extracted from

  • Strasser, R.; Stadlmann, J.; Svoboda, B.; Altmann, F.; Glossl, J.; Mach, L.
    Molecular basis of N-acetylglucosaminyltransferase I deficiency in Arabidopsis thaliana plants lacking complex N-glycans (2005), Biochem. J., 387, 385-391.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.101

Cloned(Commentary)

Cloned (Comment) Organism
expression of the mutant enzyme D144N in insect cells Arabidopsis thaliana
transformation construct contains either the catalytic domain (amino acids 106-447) of wild-type enzyme or D144N rabbit NgTI fused to the CTS region (amino acids 1-102) of Arabidopsis thaliana GnTI under the control of the strong constitutive cauliflower mosaic virus 35S promoter Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
D144N D144N muation in the GnTI of cgl mutant lacking GnTI activity is molecular basis of the defect. The mutation creates an additional N-glycosylation site, which interferes with the proper folding of the enzyme Arabidopsis thaliana
D144N expression of D144N muatant enzyme of rabbit in cgl mutant of Arabidopsis thaliana lacking GnTI activity (caused by a D144N mutation in GnTI) can partially restore complex N-glycan formation Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Oryctolagus cuniculus the enzyme is essential for processing of high-mannose to hybrid and complex N-glycans ?
-
 ?
additional information Arabidopsis thaliana the enzyme is essential for processing of high-mannose to hybrid and complex N-glycans ?
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
 a D144N muation in the GnTI of cgl mutant lacking GnTI activity is molecular basis of the defect
-
Oryctolagus cuniculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein D144N muation in the GnTI of cgl mutant lacking GnTI activity is molecular basis of the defect. The mutation creates an additional N-glycosylation site, which interferes with the proper folding of the enzyme Arabidopsis thaliana

Purification (Commentary)

Purification (Comment) Organism
mutant enzyme D144N Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is essential for processing of high-mannose to hybrid and complex N-glycans Oryctolagus cuniculus ?
-
 ?
additional information the enzyme is essential for processing of high-mannose to hybrid and complex N-glycans Arabidopsis thaliana ?
-
 ?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2-glycopeptide
-
 Oryctolagus cuniculus UDP + GlcNAc(1-2)Man5GlcNAc2-glycopeptide
-
 ?
UDP-N-acetyl-D-glucosamine + Man5GlcNAc2-glycopeptide
-
 Arabidopsis thaliana UDP + GlcNAc(1-2)Man5GlcNAc2-glycopeptide
-
 ?
UDP-N-acetyl-D-glucosamine + Manalpha1,6(Manalpha1,3)Manbeta-1-O-octyl
-
 Oryctolagus cuniculus UDP + GlcNAc(1-2)Manalpha(1-6)Manalpha(1-3)Manbeta-1-O-octyl
-
 ?
UDP-N-acetyl-D-glucosamine + Manalpha1,6(Manalpha1,3)Manbeta-1-O-octyl
-
 Arabidopsis thaliana UDP + GlcNAcalpha(1-2)Manalpha(1-6)Manalpha(1-3)Manbeta-1-O-octyl
-
 ?

Synonyms

Synonyms Comment Organism
N-acetylglucosaminyltransferase I
-
 Oryctolagus cuniculus
N-acetylglucosaminyltransferase I
-
 Arabidopsis thaliana