EC Number | Cloned (Comment) | Organism |
---|---|---|
2.4.1.101 | the organism has three different GlcNAc-TI genes: gly-12, gly-13 and gly-14 | Caenorhabditis elegans |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.4.1.101 | 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 |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.4.1.101 | Golgi membrane | - |
Caenorhabditis elegans | 139 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.101 | UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] | Caenorhabditis elegans | - |
UDP + Man5GlcNAc3-[protein] | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.1.101 | Caenorhabditis elegans | G5EBG7 | - |
- |
2.4.1.101 | Caenorhabditis elegans | G5EFK6 | - |
- |
2.4.1.101 | Caenorhabditis elegans | Q11068 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.101 | UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] | - |
Caenorhabditis elegans | UDP + Man5GlcNAc3-[protein] | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.1.101 | GlcNAc-TI | - |
Caenorhabditis elegans |
2.4.1.101 | gly-12 | - |
Caenorhabditis elegans |
2.4.1.101 | GLY-13 | - |
Caenorhabditis elegans |
2.4.1.101 | gly-14 | - |
Caenorhabditis elegans |
2.4.1.101 | MGAT1 | - |
Caenorhabditis elegans |
2.4.1.101 | N-acetylglucosaminyltransferase I | - |
Caenorhabditis elegans |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.4.1.101 | 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 |
2.4.1.101 | 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 |
2.4.1.101 | additional information | analysis of the diversity of wild-type and mutant Caenorhabditis elegans N-glycomes, profiled by MALDI-TOF MS, overview | Caenorhabditis elegans |
2.4.1.101 | 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 |