Literature summary for 2.4.1.102 extracted from

Tvaroska, I.; Kozmon, S.; Wimmerova, M.; Koca, J.
A QM/MM investigation of the catalytic mechanism of metal-ion-independent core 2 beta1,6-N-acetylglucosaminyltransferase (2013), Chemistry, 19, 8153-8162.

Search for more literature for 2.4.1.102

Cloned(Commentary)

Cloned (Comment)	Organism
gene Gcnt1	Mus musculus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
Golgi apparatus	-	Mus musculus	5794	-

Metals/Ions

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/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Mus musculus	Q09324	leukocyte-type isoform C2GnT-1, gene Gcnt1	-

Reaction

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	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
leukocyte	leukocyte-type isozyme	Mus musculus	-

Substrates and Products (Substrate)

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

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

Synonyms	Comment	Organism
C2GnT	-	Mus musculus
C2GnT-L	-	Mus musculus
core 2 beta1,6-N-acetylglucosaminyltransferase	-	Mus musculus

General Information

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)