Cloned (Comment) | Organism |
---|---|
gene Gcnt1 | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
Golgi apparatus | - |
Mus musculus | 5794 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | metal ion-independent enzyme. The enzyme does not contain the metal-ion-binding DXD pattern typical for inverting glycosyltransferases with the GT-A fold | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-N-acetyl-alpha-D-glucosamine + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R | Mus musculus | - |
UDP + beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl-R | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q09324 | leukocyte-type isoform C2GnT-1, gene Gcnt1 | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
UDP-N-acetyl-alpha-D-glucosamine + O3-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl/threonyl-[protein] = UDP + O3-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl/threonyl-[protein] | C2GnT operates through an inverting mechanism following a SN2-like reaction in which the enzyme provides a catalytic base that activates the nucleophile (in C2GnT, this is the C6 hydroxyl group from a GalNAc residue) to displace the uridine 5'-diphosphate (UDP) leaving group from the UDP-GlcNAc donor in a concerted process. It is assumed that C2GnT follows the ordered bi-bi catalytic mechanism with the UDP-GlcNAc bindings first, followed by the disaccharide acceptor binding over the nucleotide sugar. Reaction mechanism, quantum mechanical/molecular modeling, overview | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
leukocyte | leukocyte-type isozyme | Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the isozyme exhibits exclusive core 2 acceptor specificity. C2GnT operates through an inverting mechanism | Mus musculus | ? | - |
? | |
UDP-N-acetyl-alpha-D-glucosamine + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R | - |
Mus musculus | UDP + beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl-R | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | the monomer units of the observed dimer C2GnT possesses the GT-A fold and are connected by a disulfide bond between the Cys235 residues, quantum mechanical/molecular modeling using enzyme crystal structures, PDB IDs 2GAK and 2GAM, as templates. The structure of C2GnT contains two regions; the first (38-121) is composed of alpha-helices. The second region, which corresponds to the catalytic domain (122-428), is an alpha/beta/alpha structure consisting of a central six-stranded mixed beta-sheet. Four disulfide bonds are found in each monomer (Cys151-Cys199, Cys372-Cys381, Cys59-Cys413, and Cys100-Cys172), the remaining Cys217 is unpaired and located in the donor binding site. C2GnT may occur in an open conformation, and a closed conformation. The location of the C2GnT-conserved Glu320 residue structurally corresponds to the catalytic base found in other glycosyltransferases with the GT-A fold | Mus musculus |
Synonyms | Comment | Organism |
---|---|---|
C2GnT | - |
Mus musculus |
C2GnT-L | - |
Mus musculus |
core 2 beta1,6-N-acetylglucosaminyltransferase | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the GT14 family | Mus musculus |
additional information | quantum mechanical/molecular modeling using enzyme crystal structures, PDB IDs 2GAK and 2GAM, as templates. C2GnT may occur in an open conformation, and a closed conformation. The location of the C2GnT-conserved Glu320 residue structurally corresponds to the catalytic base found in other glycosyltransferases with the GT-A fold. The enzyme-substrate system (C2GnT-UDP-GlcNAc-Galb1-3GalNAc ternary complex) consists of 379 amino acids, eight water molecules, donor, and acceptor, active site model | Mus musculus |