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

BRENDA support

Literature summary for 2.4.1.101 extracted from

  • Yan, S.; Wang, H.; Schachter, H.; Jin, C.; Wilson, I.B.H.; Paschinger, K.
    Ablation of N-acetylglucosaminyltransferases in Caenorhabditis induces expression of unusual intersected and bisected N-glycans (2018), Biochim. Biophys. Acta, 1862, 2191-2203 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.101

Cloned(Commentary)

Cloned (Comment) Organism
the organism has three different GlcNAc-TI genes: gly-12, gly-13 and gly-14 Caenorhabditis elegans

Protein Variants

Protein Variants Comment Organism
additional information complete abolition of GlcNAc-TI activity requires the generation of a triple knock-out strain, knockoing out the three genes encoding the enzyme, i.e. gly-12, gly-13 and gly-14. The multiple hexose residues of the N-glycans of the gly-12/gly-13/gly-14 triple mutant are not just mannose, but include galactoses in three different positions (beta-intersecting, beta-bisecting and alpha-terminal) on isomeric forms of Hex4-8HexNAc2 structures, some of these structures are fucosylated and/or methylated, determination of the N-glycome of 12/gly-13/gly-14 triple GlcNAc-TI knock-out strain Caenorhabditis elegans

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi membrane
-
 Caenorhabditis elegans 139
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] Caenorhabditis elegans
-
 UDP + Man5GlcNAc3-[protein]
-
 ?

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans G5EBG7
-
-
Caenorhabditis elegans G5EFK6
-
-
Caenorhabditis elegans Q11068
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein]
-
 Caenorhabditis elegans UDP + Man5GlcNAc3-[protein]
-
 ?

Synonyms

Synonyms Comment Organism
GlcNAc-TI
-
 Caenorhabditis elegans
gly-12
-
 Caenorhabditis elegans
GLY-13
-
 Caenorhabditis elegans
gly-14
-
 Caenorhabditis elegans
MGAT1
-
 Caenorhabditis elegans
N-acetylglucosaminyltransferase I
-
 Caenorhabditis elegans

General Information

General Information Comment Organism
evolution the modification in the Golgi of N-glycans by N-acetylglucosaminyltransferase I (GlcNAc-TI, MGAT1) can be considered to be a hallmark of multicellular eukaryotes as it is found in all metazoans and plants, but rarely in unicellular organisms Caenorhabditis elegans
metabolism the N-glycomic repertoire of Caenorhabditis exhibits a large degree of plasticity even in the absence of key glycan processing enzymes from the Golgi apparatus Caenorhabditis elegans
additional information analysis of the diversity of wild-type and mutant Caenorhabditis elegans N-glycomes, profiled by MALDI-TOF MS, overview Caenorhabditis elegans
physiological function the modification in the Golgi of N-glycans is catalyzed by N-acetylglucosaminyltransferase I (GlcNAc-TI, MGAT1). The enzyme is key for the normal processing of N-glycans to either complex or paucimannosidic forms, both of which are found in the model nematode Caenorhabditis elegans Caenorhabditis elegans