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

BRENDA support

Literature summary for 2.4.1.101 extracted from

  • Henquet, M.; Heinhuis, B.; Borst, J.; Eigenhuijsen, J.; Schreuder, M.; Bosch, D.; van der Krol, A.
    Differential effects of human and plant N-acetylglucosaminyltransferase I (GnTI) in plants (2009), Transgenic Res., 19, 535-547.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.101

Cloned(Commentary)

Cloned (Comment) Organism
expression of YFP or CFP fusion enzyme of Arabidopsis and human N-acetylglucosaminyltransferase I, and the chimeric enzyme of Arabidopsis CTS region and human catalytic domain in mutant cgl1-1 Arabidopsis (lacking N-acetylglucosaminyltransferase I), transformed by Agrobacterium tumefaciens Homo sapiens
expression of YFP or CFP fusion enzyme of Arabidopsis and human N-acetylglucosaminyltransferase I, and the chimeric enzyme of Arabidopsis CTS region and human catalytic domain in mutant cgl1-1 Arabidopsis (lacking N-acetylglucosaminyltransferase I), transformed by Agrobacterium tumefaciens Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information Elisa experiments show that cgl1-1 mutant of Arabidopsis lacking N-acetylglucosaminyltransferase I activity, is fully complemented by YFP-labeled Arabidopsis enzyme (similar level of proteins with complex glycans), but only partially complemented by human enzyme (lower levels of proteins with complex glycans), chimeric enzyme with similar levels compared to wild-type, sub-cellular localization of the human enzyme is partly distinct, the human enzyme is easily cleaved of its transmembrane anchor Homo sapiens
additional information Elisa experiments show that cgl1-1 mutant of Arabidopsis lacking N-acetylglucosaminyltransferase I activity, is fully complemented by YFP-labeled Arabidopsis enzyme (similar level of proteins with complex glycans), but only partially complemented by human enzyme (lower levels of proteins with complex glycans), chimeric enzyme with similar levels compared to wild-type, sub-cellular localization of the human enzyme is partly distinct, the human enzyme is easily cleaved of its transmembrane anchor Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi membrane
-
 Arabidopsis thaliana 139
-
additional information mesophyll protoplasts are created to analyze differences in localization Arabidopsis thaliana
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
78000
-
 mass of the fusion protein, free YFP-marker is about 27000 Da, SDS-PAGE Homo sapiens
78000
-
 mass of the fusion protein, free YFP-marker is about 27000 Da, SDS-PAGE Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Arabidopsis thaliana
-

Synonyms

Synonyms Comment Organism
AtGnTI Arabidopsis enzyme Arabidopsis thaliana
ChGnTI chimeric Arabidopsis-human enzyme Homo sapiens
ChGnTI chimeric Arabidopsis-human enzyme Arabidopsis thaliana
GnTI
-
 Homo sapiens
GnTI
-
 Arabidopsis thaliana
HuGnTI human enzyme Homo sapiens
N-acetylglucosaminyltransferase I
-
 Homo sapiens
N-acetylglucosaminyltransferase I
-
 Arabidopsis thaliana

Expression

Organism Comment Expression
Arabidopsis thaliana human fusion enzyme expression is about 5fold higher in Arabidopsis cgl1-1 mutant than Arabidopsis and chimeric enzyme expression but lower catalytic activity in the plant and partly distinct sub-cellular localization additional information
Homo sapiens human fusion enzyme expression is about 5fold higher in Arabidopsis than Arabidopsis enzyme and chimeric enzyme expression but catalytic activity in the plant is lower and shows partly distinct sub-cellular localization additional information

General Information

General Information Comment Organism
physiological function N-glycan formation on glycoproteins Homo sapiens
physiological function N-glycan formation on glycoproteins Arabidopsis thaliana